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1n99

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[[Image:1n99.gif|left|200px]]
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{{Structure
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|GENE= SDCBP OR MDA9 OR SYCL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n99 OCA], [http://www.ebi.ac.uk/pdbsum/1n99 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n99 RCSB]</span>
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'''CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN'''
'''CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN'''
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[[Category: Kang, B S.]]
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[[Category: Otlewski, J.]]
[[Category: Otlewski, J.]]
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[[Category: pdz domain]]
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Revision as of 23:15, 2 May 2008

Template:STRUCTURE 1n99

CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN


Overview

Syntenin, a 33 kDa protein, interacts with several cell membrane receptors and with merlin, the product of the causal gene for neurofibromatosis type II. We report a crystal structure of the functional fragment of human syntenin containing two canonical PDZ domains, as well as binding studies for full-length syntenin, the PDZ tandem, and isolated PDZ domains. We show that the functional properties of syntenin are a result of independent interactions with target peptides, and that each domain is able to bind peptides belonging to two different classes: PDZ1 binds peptides from classes I and III, while PDZ2 interacts with classes I and II. The independent binding of merlin by PDZ1 and syndecan-4 by PDZ2 provides direct evidence for the coupling of syndecan-mediated signaling to actin regulation by merlin.

About this Structure

1N99 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

PDZ tandem of human syntenin: crystal structure and functional properties., Kang BS, Cooper DR, Jelen F, Devedjiev Y, Derewenda U, Dauter Z, Otlewski J, Derewenda ZS, Structure. 2003 Apr;11(4):459-68. PMID:12679023 Page seeded by OCA on Sat May 3 02:15:16 2008

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