1qau
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qau OCA], [http://www.ebi.ac.uk/pdbsum/1qau PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qau RCSB]</span> | ||
}} | }} | ||
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[[Category: beta-finger]] | [[Category: beta-finger]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:11:09 2008'' |
Revision as of 20:11, 30 March 2008
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| , resolution 1.25Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
About this Structure
1QAU is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
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
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