PDZ tandem of human syntenin: Crystal structure and functional properties

被引:95
作者
Kang, BS
Cooper, DR
Jelen, F
Devedjiev, Y
Derewenda, U
Dauter, Z
Otlewski, J
Derewenda, ZS [1 ]
机构
[1] Univ Virginia, Ctr Canc, Dept Mol Physiol & Biol Phys, Charlottesville, VA 22908 USA
[2] Univ Wroclaw, Inst Biochem & Mol Biol, Lab Prot Engn, PL-50137 Wroclaw, Poland
[3] NCI, Synchrotron Radiat Res Stn, Macromol Crystallog Lab, Brookhaven Natl Lab, Upton, NY 11973 USA
关键词
PDZ; syndecan; merlin; schwannoma; cancer; crystallography; calorimetry;
D O I
10.1016/S0969-2126(03)00052-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:459 / 468
页数:10
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