1n99
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(New page: 200px<br /> <applet load="1n99" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n99, resolution 1.94Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 16:12, 12 November 2007
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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
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