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PDZ tandem of human syntenin: crystal structure and functional properties.

Abstract
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.
AuthorsBeom Sik Kang, David R Cooper, Filip Jelen, Yancho Devedjiev, Urszula Derewenda, Zbigniew Dauter, Jacek Otlewski, Zygmunt S Derewenda
JournalStructure (London, England : 1993) (Structure) Vol. 11 Issue 4 Pg. 459-68 (Apr 2003) ISSN: 0969-2126 [Print] United States
PMID12679023 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S.)
Chemical References
  • Actins
  • Carrier Proteins
  • Intracellular Signaling Peptides and Proteins
  • Membrane Glycoproteins
  • Membrane Proteins
  • Neurofibromin 2
  • Peptide Fragments
  • Proteoglycans
  • SDCBP protein, human
  • Syndecans
  • Syntenins
Topics
  • Actins (metabolism)
  • Amino Acid Sequence
  • Animals
  • Carrier Proteins (chemistry, genetics, metabolism)
  • Crystallography, X-Ray
  • Cytoskeleton (metabolism)
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • Membrane Glycoproteins (metabolism)
  • Membrane Proteins (chemistry, genetics, metabolism)
  • Models, Molecular
  • Molecular Sequence Data
  • Neurofibromin 2 (chemistry, metabolism)
  • Peptide Fragments (chemistry, genetics, metabolism)
  • Protein Binding
  • Protein Structure, Tertiary
  • Proteoglycans (metabolism)
  • Sequence Alignment
  • Syndecans
  • Syntenins

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