Difference: XiangpengKong (1 vs. 7)
Revision 702 Apr 2009 - Main.SherryllJones
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| < < | Grant Number: 5P01DK052206-090003 | |||||||||||||||||||||||||||||||||||||||||||||||
| > > | Grant Number: 5P01DK052206-090003 Project Title: Structural Biology of Urothelial Membranes PI Information: Name Email Title KONG, XIANGPENG kong@saturn.med.nyu.edu PROFESSOR | |||||||||||||||||||||||||||||||||||||||||||||||
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| < < | Project Title: Structural Biology of Urothelial Membranes | |||||||||||||||||||||||||||||||||||||||||||||||
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| < < | PI Information: Name Email Title KONG, XIANGPENG kong@saturn.med.nyu.edu PROFESSOR | |||||||||||||||||||||||||||||||||||||||||||||||
| Abstract: The apical surface of bladder epithelium is covered by rigid-looking plaques consisting of hexagonally packed crystalline arrays of 16 nm protein particles made up of four major uroplakins (UPs). These urothelial plaques serve as an effective permeability barrier, and may play a role in the reversible adjustment of the urothelial apical surface area during different phases of the micturition cycle, In addition, the attachment of uropathogenic type 1-piliated E. coli to their uroplakin Ia receptor can cause urothelial cytoskeletal rearrangement, apoptosis and bacterial invasion. The goal of this project is to understand the structural basis of urothelial plaque functions. Based on our recently obtained 10 Angstrom resolution cryo-EM structure of the 16 nm mouse urothelial particles, we hypothesize that (i) the two uroplakin pairs, i.e., UPIa/II and UPIb/III, occupy the inner and outer six subdomains of the 16 nm particle, respectively, and that (ii) the relatively flexible structure of the 16 nm uroplakin particle can mediate transmembrane signal transduction through conformational changes. To test these hypotheses and to further understand the structure-function relationship of the urothelial plaques, we will perform three series of studies that will: (1) visualize the individual transmembrane helices of the uroplakins by obtaining a cryo-EM structure of the 16nm particle at the resolution range of 7 Angstroms dock the atomic models of UPIa and Ib into the cryo-EM density maps thus improving the 3D modeling, and prepare 3D crystals of uroplakins aiming at solving uroplakin strucure to atomic resolution; (2) localize in the 3D architecture of the 16 nm particle several uroplakin moieties using Fab fragments and specific lectins as the probes; and (3) study the possible bacterial binding-induced conformational changes of the 16 nm uroplakin particle by comparing the 3D cryo-EM structures of the particle in the presence and absence of saturating amounts of the bacterial adhesin FimH?. Our results should lead to a better understanding of the structural bases of urothelial plaque function, and of the possible roles of urothelial plaques in urinary tract infection. Thesaurus Terms: apical membrane, kidney function, membrane activity, membrane protein, membrane structure, urinary bladder epithelium biological signal transduction, protein localization, protein structure function, structural biology SDS polyacrylamide gel electrophoresis, X ray crystallography, computer simulation, cryoelectron microscopy, crystallization, image processing, scanning transmission electron microscopy Institution: NEW YORK UNIVERSITY SCHOOL OF MEDICINE NEW YORK, NY 10016 Fiscal Year: 2007 Department: Project Start: 01-JUL-2007 Project End: 30-JUN-2009 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: ZDK1 | ||||||||||||||||||||||||||||||||||||||||||||||||
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| > > | Grant Number: 5R01GM070841-04 Project Title: Structures of priming and recombination complexes PI Information: Name Email Title KONG, XIANGPENG kong@saturn.med.nyu.edu PROFESSOR | |||||||||||||||||||||||||||||||||||||||||||||||
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| > > | Abstract: DESCRIPTION (provided by applicant): The continuous movement of the DNA replication fork requires priming at the lagging strand to make each Okazaki fragment, as well as a coordinated action of primases and the replicative DNA polymerase. The replication origin of the single-stranded DNA (ssDNA) bacteriophage G4 (G4ori) is a simple system of priming for DNA replication; it needs only the E. coli primase (dnaG) and the single-stranded DNA binding protein (SSB). G4ori consists of three stem-loops located immediately on the 5' side of the initiation trinucleotide 5'-CTG-3' and, upon saturated binding by SSB tetramers, will form a unique structure recognizable by dnaG primase. The three domains of the modular primase then bind the G4ori initiation site cooperatively to synthesize the primer RNA. A 278 nucleotide fragment of G4ori (G4ori278), together with two dnaG primases and four SSB tetramers, can form a minimal active priming complex suitable for structural investigations. The continuous movement of the replication fork also requires recombinational repair at sites of DNA damage and recFOR complexes of the recF recombination pathway are mediators of replication and recombination. Structural information of these replication and recombination complexes will help us understand the function of the replication machineries. Toward this goal, we propose three sets of experiments: 1) To determine the X-ray structures of the two-component complex of SSB-G4ori278 and a complex of SSB with a fragment of the lacZ gene. These structures will help us understand the structural formation of the functional G4ori, as well as SSB's modes of ssDNA-binding. 2) To determine the X-ray structure of the three-component complex of primase-SSB-G4ori278, which will reveal details of the primase- G4ori interaction, as well as the primase-SSB interaction. 3) To determine the X-ray structure of recR and to crystallize other proteins, as well as complexes in the recF pathway. Obtaining the structural information of these proteins and complexes will serve as an important step in understanding the recombinational repair. Public Health Relevance: This Public Health Relevance is not available. Thesaurus Terms: DNA binding protein, DNA primase, DNA replication, bacterial virus, crystallization, genetic recombination, protein protein interaction, protein structure function, recombinase, structural biology DNA damage X ray crystallography Institution: NEW YORK UNIVERSITY SCHOOL OF MEDICINE 550 1ST AVE NEW YORK, NY 10016 Fiscal Year: 2008 Department: SKIRBALL INSTITUTE OF BIOMOLECULAR MEDICINE Project Start: 01-FEB-2005 Project End: 31-JAN-2010 ICD: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES IRG: BBCA | |||||||||||||||||||||||||||||||||||||||||||||||
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Revision 601 Apr 2008 - Main.DavidCowburn
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Public information from CRISP Grant Number: 5P01DK052206-090003 Project Title: Structural Biology of Urothelial Membranes PI Information: Name Email Title KONG, XIANGPENG kong@saturn.med.nyu.edu PROFESSOR | ||||||||||||||||||||||||||||||||||||||||||||||||||
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| < < | Abstract: The apical surface of bladder epithelium is covered by rigid-looking plaques consisting of hexagonally packed crystalline arrays of 16 nm protein particles made up of four major uroplakins (UPs). These urothelial plaques serve as an effective permeability barrier, and may play a role in the reversible adjustment of the urothelial apical surface area during different phases of the micturition cycle, In addition, the attachment of uropathogenic type 1-piliated E. coli to their uroplakin Ia receptor can cause urothelial cytoskeletal rearrangement, apoptosis and bacterial invasion. The goal of this projectyiyiu is to understand the structural basis of urothelial plaque functions. Based on our recently obtained 10 Angstrom resolution cryo-EM structure of the 16 nm mouse urothelial particles, we hypothesize that (i) the two uroplakin pairs, i.e., UPIa/II and UPIb/III, occupy the inner and outer six subdomains of the 16 nm particle, respectively, and that (ii) the relatively flexible structure of the 16 nm uroplakin particle can mediate transmembrane signal transduction through conformational changes. To test these hypotheses and to further understand the structure-function relationship of the urothelial plaques, we will perform three series of studies that will: (1) visualize the individual transmembrane helices of the uroplakins by obtaining a cryo-EM structure of the 16nm particle at the resolution range of 7 Angstroms dock the atomic models of UPIa and Ib into the cryo-EM density maps thus improving the 3D modeling, and prepare 3D crystals of uroplakins aiming at solving uroplakin strucure to atomic resolution; (2) localize in the 3D architecture of the 16 nm particle several uroplakin moieties using Fab fragments and specific lectins as the probes; and (3) study the possible bacterial binding-induced conformational changes of the 16 nm uroplakin particle by comparing the 3D cryo-EM structures of the particle in the presence and absence of saturating amounts of the bacterial adhesin FimH?. Our results should lead to a better understanding of the structural bases of urothelial plaque function, and of the possible roles of urothelial plaques in urinary tract infection. | |||||||||||||||||||||||||||||||||||||||||||||||||
| > > | Abstract: The apical surface of bladder epithelium is covered by rigid-looking plaques consisting of hexagonally packed crystalline arrays of 16 nm protein particles made up of four major uroplakins (UPs). These urothelial plaques serve as an effective permeability barrier, and may play a role in the reversible adjustment of the urothelial apical surface area during different phases of the micturition cycle, In addition, the attachment of uropathogenic type 1-piliated E. coli to their uroplakin Ia receptor can cause urothelial cytoskeletal rearrangement, apoptosis and bacterial invasion. The goal of this project is to understand the structural basis of urothelial plaque functions. Based on our recently obtained 10 Angstrom resolution cryo-EM structure of the 16 nm mouse urothelial particles, we hypothesize that (i) the two uroplakin pairs, i.e., UPIa/II and UPIb/III, occupy the inner and outer six subdomains of the 16 nm particle, respectively, and that (ii) the relatively flexible structure of the 16 nm uroplakin particle can mediate transmembrane signal transduction through conformational changes. To test these hypotheses and to further understand the structure-function relationship of the urothelial plaques, we will perform three series of studies that will: (1) visualize the individual transmembrane helices of the uroplakins by obtaining a cryo-EM structure of the 16nm particle at the resolution range of 7 Angstroms dock the atomic models of UPIa and Ib into the cryo-EM density maps thus improving the 3D modeling, and prepare 3D crystals of uroplakins aiming at solving uroplakin strucure to atomic resolution; (2) localize in the 3D architecture of the 16 nm particle several uroplakin moieties using Fab fragments and specific lectins as the probes; and (3) study the possible bacterial binding-induced conformational changes of the 16 nm uroplakin particle by comparing the 3D cryo-EM structures of the particle in the presence and absence of saturating amounts of the bacterial adhesin FimH?. Our results should lead to a better understanding of the structural bases of urothelial plaque function, and of the possible roles of urothelial plaques in urinary tract infection. | |||||||||||||||||||||||||||||||||||||||||||||||||
Thesaurus Terms:
apical membrane, kidney function, membrane activity, membrane protein, membrane structure, urinary bladder epithelium
biological signal transduction, protein localization, protein structure function, structural biology
SDS polyacrylamide gel electrophoresis, X ray crystallography, computer simulation, cryoelectron microscopy, crystallization, image processing, scanning transmission electron microscopy
Institution: NEW YORK UNIVERSITY SCHOOL OF MEDICINE
NEW YORK, NY 10016
Fiscal Year: 2007
Department:
Project Start: 01-JUL-2007
Project End: 30-JUN-2009
ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES
IRG: ZDK1
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Revision 521 Mar 2008 - Main.DavidCowburn
My Links
Personal PreferencesUncomment preferences variables to activate them (remove the #-sign). Help and details on preferences variables are available in TWikiPreferences.
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Public information from CRISP Grant Number: 5P01DK052206-090003 Project Title: Structural Biology of Urothelial Membranes PI Information: Name Email Title KONG, XIANGPENG kong@saturn.med.nyu.edu PROFESSOR | ||||||||||||||||||||||||||||||||||||||||||||||||||
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| < < | Abstract: The apical surface of bladder epithelium is covered by rigid-looking plaques consisting of hexagonally packed crystalline arrays of 16 nm protein particles made up of four major uroplakins (UPs). These urothelial plaques serve as an effective permeability barrier, and may play a role in the reversible adjustment of the urothelial apical surface area during different phases of the micturition cycle, In addition, the attachment of uropathogenic type 1-piliated E. coli to their uroplakin Ia receptor can cause urothelial cytoskeletal rearrangement, apoptosis and bacterial invasion. The goal of this project is to understand the structural basis of urothelial plaque functions. Based on our recently obtained 10 Angstrom resolution cryo-EM structure of the 16 nm mouse urothelial particles, we hypothesize that (i) the two uroplakin pairs, i.e., UPIa/II and UPIb/III, occupy the inner and outer six subdomains of the 16 nm particle, respectively, and that (ii) the relatively flexible structure of the 16 nm uroplakin particle can mediate transmembrane signal transduction through conformational changes. To test these hypotheses and to further understand the structure-function relationship of the urothelial plaques, we will perform three series of studies that will: (1) visualize the individual transmembrane helices of the uroplakins by obtaining a cryo-EM structure of the 16nm particle at the resolution range of 7 Angstroms dock the atomic models of UPIa and Ib into the cryo-EM density maps thus improving the 3D modeling, and prepare 3D crystals of uroplakins aiming at solving uroplakin strucure to atomic resolution; (2) localize in the 3D architecture of the 16 nm particle several uroplakin moieties using Fab fragments and specific lectins as the probes; and (3) study the possible bacterial binding-induced conformational changes of the 16 nm uroplakin particle by comparing the 3D cryo-EM structures of the particle in the presence and absence of saturating amounts of the bacterial adhesin FimH?. Our results should lead to a better understanding of the structural bases of urothelial plaque function, and of the possible roles of urothelial plaques in urinary tract infection. | |||||||||||||||||||||||||||||||||||||||||||||||||
| > > | Abstract: The apical surface of bladder epithelium is covered by rigid-looking plaques consisting of hexagonally packed crystalline arrays of 16 nm protein particles made up of four major uroplakins (UPs). These urothelial plaques serve as an effective permeability barrier, and may play a role in the reversible adjustment of the urothelial apical surface area during different phases of the micturition cycle, In addition, the attachment of uropathogenic type 1-piliated E. coli to their uroplakin Ia receptor can cause urothelial cytoskeletal rearrangement, apoptosis and bacterial invasion. The goal of this projectyiyiu is to understand the structural basis of urothelial plaque functions. Based on our recently obtained 10 Angstrom resolution cryo-EM structure of the 16 nm mouse urothelial particles, we hypothesize that (i) the two uroplakin pairs, i.e., UPIa/II and UPIb/III, occupy the inner and outer six subdomains of the 16 nm particle, respectively, and that (ii) the relatively flexible structure of the 16 nm uroplakin particle can mediate transmembrane signal transduction through conformational changes. To test these hypotheses and to further understand the structure-function relationship of the urothelial plaques, we will perform three series of studies that will: (1) visualize the individual transmembrane helices of the uroplakins by obtaining a cryo-EM structure of the 16nm particle at the resolution range of 7 Angstroms dock the atomic models of UPIa and Ib into the cryo-EM density maps thus improving the 3D modeling, and prepare 3D crystals of uroplakins aiming at solving uroplakin strucure to atomic resolution; (2) localize in the 3D architecture of the 16 nm particle several uroplakin moieties using Fab fragments and specific lectins as the probes; and (3) study the possible bacterial binding-induced conformational changes of the 16 nm uroplakin particle by comparing the 3D cryo-EM structures of the particle in the presence and absence of saturating amounts of the bacterial adhesin FimH?. Our results should lead to a better understanding of the structural bases of urothelial plaque function, and of the possible roles of urothelial plaques in urinary tract infection. | |||||||||||||||||||||||||||||||||||||||||||||||||
Thesaurus Terms:
apical membrane, kidney function, membrane activity, membrane protein, membrane structure, urinary bladder epithelium
biological signal transduction, protein localization, protein structure function, structural biology
SDS polyacrylamide gel electrophoresis, X ray crystallography, computer simulation, cryoelectron microscopy, crystallization, image processing, scanning transmission electron microscopy
Institution: NEW YORK UNIVERSITY SCHOOL OF MEDICINE
NEW YORK, NY 10016
Fiscal Year: 2007
Department:
Project Start: 01-JUL-2007
Project End: 30-JUN-2009
ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES
IRG: ZDK1
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Revision 406 Mar 2008 - Main.DavidCowburn
My Links
Personal PreferencesUncomment preferences variables to activate them (remove the #-sign). Help and details on preferences variables are available in TWikiPreferences.
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| Added: | ||||||||||||||||||||||||||||||||||||||||||||||||||
| > > | Public information from CRISP Grant Number: 5P01DK052206-090003 Project Title: Structural Biology of Urothelial Membranes PI Information: Name Email Title KONG, XIANGPENG kong@saturn.med.nyu.edu PROFESSOR Abstract: The apical surface of bladder epithelium is covered by rigid-looking plaques consisting of hexagonally packed crystalline arrays of 16 nm protein particles made up of four major uroplakins (UPs). These urothelial plaques serve as an effective permeability barrier, and may play a role in the reversible adjustment of the urothelial apical surface area during different phases of the micturition cycle, In addition, the attachment of uropathogenic type 1-piliated E. coli to their uroplakin Ia receptor can cause urothelial cytoskeletal rearrangement, apoptosis and bacterial invasion. The goal of this project is to understand the structural basis of urothelial plaque functions. Based on our recently obtained 10 Angstrom resolution cryo-EM structure of the 16 nm mouse urothelial particles, we hypothesize that (i) the two uroplakin pairs, i.e., UPIa/II and UPIb/III, occupy the inner and outer six subdomains of the 16 nm particle, respectively, and that (ii) the relatively flexible structure of the 16 nm uroplakin particle can mediate transmembrane signal transduction through conformational changes. To test these hypotheses and to further understand the structure-function relationship of the urothelial plaques, we will perform three series of studies that will: (1) visualize the individual transmembrane helices of the uroplakins by obtaining a cryo-EM structure of the 16nm particle at the resolution range of 7 Angstroms dock the atomic models of UPIa and Ib into the cryo-EM density maps thus improving the 3D modeling, and prepare 3D crystals of uroplakins aiming at solving uroplakin strucure to atomic resolution; (2) localize in the 3D architecture of the 16 nm particle several uroplakin moieties using Fab fragments and specific lectins as the probes; and (3) study the possible bacterial binding-induced conformational changes of the 16 nm uroplakin particle by comparing the 3D cryo-EM structures of the particle in the presence and absence of saturating amounts of the bacterial adhesin FimH?. Our results should lead to a better understanding of the structural bases of urothelial plaque function, and of the possible roles of urothelial plaques in urinary tract infection. Thesaurus Terms: apical membrane, kidney function, membrane activity, membrane protein, membrane structure, urinary bladder epithelium biological signal transduction, protein localization, protein structure function, structural biology SDS polyacrylamide gel electrophoresis, X ray crystallography, computer simulation, cryoelectron microscopy, crystallization, image processing, scanning transmission electron microscopy Institution: NEW YORK UNIVERSITY SCHOOL OF MEDICINE NEW YORK, NY 10016 Fiscal Year: 2007 Department: Project Start: 01-JUL-2007 Project End: 30-JUN-2009 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: ZDK1 | |||||||||||||||||||||||||||||||||||||||||||||||||
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Revision 319 Aug 2007 - Main.DavidCowburn
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Revision 219 Jul 2007 - Main.DavidCowburn
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Revision 119 Jul 2007 - Main.TWikiRegistrationAgent
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