1qav: Difference between revisions

Revision as of 11:06, 28 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:1qav.png

Template:STRUCTURE 1qav

UNEXPECTED MODES OF PDZ DOMAIN SCAFFOLDING REVEALED BY STRUCTURE OF NNOS-SYNTROPHIN COMPLEXUNEXPECTED MODES OF PDZ DOMAIN SCAFFOLDING REVEALED BY STRUCTURE OF NNOS-SYNTROPHIN COMPLEX

Template:ABSTRACT PUBMED 10221915

About this StructureAbout this Structure

1QAV is a Protein complex structure of sequences from Mus musculus and Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex., Hillier BJ, Christopherson KS, Prehoda KE, Bredt DS, Lim WA, Science. 1999 Apr 30;284(5415):812-5. PMID:10221915

Page seeded by OCA on Mon Jul 28 11:06:22 2008

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

OCA

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-'''UNEXPECTED MODES OF PDZ DOMAIN SCAFFOLDING REVEALED BY STRUCTURE OF NNOS-SYNTROPHIN COMPLEX'''
+===UNEXPECTED MODES OF PDZ DOMAIN SCAFFOLDING REVEALED BY STRUCTURE OF NNOS-SYNTROPHIN COMPLEX===
-==Overview==
+<!--
-The PDZ protein interaction domain of neuronal nitric oxide synthase (nNOS) can heterodimerize with the PDZ domains of postsynaptic density protein 95 and syntrophin through interactions that are not mediated by recognition of a typical carboxyl-terminal motif. The nNOS-syntrophin PDZ complex structure revealed that the domains interact in an unusual linear head-to-tail arrangement. The nNOS PDZ domain has two opposite interaction surfaces-one face has the canonical peptide binding groove, whereas the other has a beta-hairpin "finger." This nNOS beta finger docks in the syntrophin peptide binding groove, mimicking a peptide ligand, except that a sharp beta turn replaces the normally required carboxyl terminus. This structure explains how PDZ domains can participate in diverse interaction modes to assemble protein networks.
+The line below this paragraph, {{ABSTRACT_PUBMED_10221915}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_10221915}}
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 [[Category: Beta-finger]]
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