1bfe

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
==Overview==
==Overview==
-
Modular PDZ domains, found in many cell junction-associated proteins, mediate the clustering of membrane ion channels by binding to their, C-terminus. The X-ray crystallographic structures of the third PDZ domain, from the synaptic protein PSD-95 in complex with and in the absence of its, peptide ligand have been determined at 1.8 angstroms and 2.3 angstroms, resolution, respectively. The structures reveal that a four-residue, C-terminal stretch (X-Thr/Ser-X-Val-COO(-)) engages the PDZ domain through, antiparallel main chain interactions with a beta sheet of the domain., Recognition of the terminal carboxylate group of the peptide is conferred, by a cradle of main chain amides provided by a Gly-Leu-Gly-Phe loop as, well as by an arginine side chain. Specific side chain interactions and a, prominent hydrophobic pocket explain the selective recognition of the, C-terminal consensus sequence.
+
Modular PDZ domains, found in many cell junction-associated proteins, mediate the clustering of membrane ion channels by binding to their C-terminus. The X-ray crystallographic structures of the third PDZ domain from the synaptic protein PSD-95 in complex with and in the absence of its peptide ligand have been determined at 1.8 angstroms and 2.3 angstroms resolution, respectively. The structures reveal that a four-residue C-terminal stretch (X-Thr/Ser-X-Val-COO(-)) engages the PDZ domain through antiparallel main chain interactions with a beta sheet of the domain. Recognition of the terminal carboxylate group of the peptide is conferred by a cradle of main chain amides provided by a Gly-Leu-Gly-Phe loop as well as by an arginine side chain. Specific side chain interactions and a prominent hydrophobic pocket explain the selective recognition of the C-terminal consensus sequence.
==About this Structure==
==About this Structure==
Line 13: Line 13:
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Doyle, D.A.]]
+
[[Category: Doyle, D A.]]
[[Category: Kim, E.]]
[[Category: Kim, E.]]
[[Category: Lee, A.]]
[[Category: Lee, A.]]
Line 22: Line 22:
[[Category: protein localization]]
[[Category: protein localization]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:32:49 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:54:40 2008''

Revision as of 09:54, 21 February 2008


1bfe, resolution 2.3Å

Drag the structure with the mouse to rotate

THE THIRD PDZ DOMAIN FROM THE SYNAPTIC PROTEIN PSD-95

Overview

Modular PDZ domains, found in many cell junction-associated proteins, mediate the clustering of membrane ion channels by binding to their C-terminus. The X-ray crystallographic structures of the third PDZ domain from the synaptic protein PSD-95 in complex with and in the absence of its peptide ligand have been determined at 1.8 angstroms and 2.3 angstroms resolution, respectively. The structures reveal that a four-residue C-terminal stretch (X-Thr/Ser-X-Val-COO(-)) engages the PDZ domain through antiparallel main chain interactions with a beta sheet of the domain. Recognition of the terminal carboxylate group of the peptide is conferred by a cradle of main chain amides provided by a Gly-Leu-Gly-Phe loop as well as by an arginine side chain. Specific side chain interactions and a prominent hydrophobic pocket explain the selective recognition of the C-terminal consensus sequence.

About this Structure

1BFE is a Single protein structure of sequence from Rattus norvegicus. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ., Doyle DA, Lee A, Lewis J, Kim E, Sheng M, MacKinnon R, Cell. 1996 Jun 28;85(7):1067-76. PMID:8674113

Page seeded by OCA on Thu Feb 21 11:54:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools