1i92: Difference between revisions

Revision as of 10:36, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1i92.png

Template:STRUCTURE 1i92

STRUCTURAL BASIS OF THE NHERF PDZ1-CFTR INTERACTIONSTRUCTURAL BASIS OF THE NHERF PDZ1-CFTR INTERACTION

Template:ABSTRACT PUBMED 11304524

About this StructureAbout this Structure

1I92 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis of the Na+/H+ exchanger regulatory factor PDZ1 interaction with the carboxyl-terminal region of the cystic fibrosis transmembrane conductance regulator., Karthikeyan S, Leung T, Ladias JA, J Biol Chem. 2001 Jun 8;276(23):19683-6. Epub 2001 Apr 13. PMID:11304524

Page seeded by OCA on Tue Jul 1 10:36:16 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1i92.gif|left|200px]]
+{{Seed}}
+[[Image:1i92.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1i92|  PDB=1i92  |  SCENE=  }}
-'''STRUCTURAL BASIS OF THE NHERF PDZ1-CFTR INTERACTION'''
+===STRUCTURAL BASIS OF THE NHERF PDZ1-CFTR INTERACTION===
-==Overview==
+<!--
-The PDZ1 domain of the Na(+)/H(+) exchanger regulatory factor (NHERF) binds with nanomolar affinity to the carboxyl-terminal sequence QDTRL of the cystic fibrosis transmembrane conductance regulator (CFTR) and plays a central role in the cellular localization and physiological regulation of this chloride channel. The crystal structure of human NHERF PDZ1 bound to the carboxyl-terminal peptide QDTRL has been determined at 1.7-A resolution. The structure reveals the specificity and affinity determinants of the PDZ1-CFTR interaction and provides insights into carboxyl-terminal leucine recognition by class I PDZ domains. The peptide ligand inserts into the PDZ1 binding pocket forming an additional antiparallel beta-strand to the PDZ1 beta-sheet, and an extensive network of hydrogen bonds and hydrophobic interactions stabilize the complex. Remarkably, the guanido group of arginine at position -1 of the CFTR peptide forms two salt bridges and two hydrogen bonds with PDZ1 residues Glu(43) and Asn(22), respectively, providing the structural basis for the contribution of the penultimate amino acid of the peptide ligand to the affinity of the interaction.
+The line below this paragraph, {{ABSTRACT_PUBMED_11304524}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11304524 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11304524}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Nherf]]
 [[Category: Pdz]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:43:24 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 10:36:16 2008''