1N99

CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN

Summary for 1N99

• Entry DOI: 10.2210/pdb1n99/pdb
• Descriptor: Syntenin 1 (2 entities in total)
• Functional Keywords: pdz domain, signaling protein
• Biological source: Homo sapiens (human)
• Cellular location: Cell junction, focal adhesion: O00560
• Total number of polymer chains: 2
• Total formula weight: 36412.54

Authors

Kang, B.S.,Cooper, D.R.,Jelen, F.,Devedjiev, Y.,Derewenda, U.,Dauter, Z.,Otlewski, J.,Derewenda, Z.S. (deposition date: 2002-11-22, release date: 2003-04-15, Last modification date: 2024-11-06)

Primary citation

Kang, B.S.,Cooper, D.R.,Jelen, F.,Devedjiev, Y.,Derewenda, U.,Dauter, Z.,Otlewski, J.,Derewenda, Z.S.
PDZ Tandem of Human Syntenin: Crystal Structure and Functional Properties
Structure, 11:459-468, 2003

PubMed 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.

PubMed: 12679023
DOI: 10.1016/S0969-2126(03)00052-2

Experimental method

X-RAY DIFFRACTION (1.94 Å)