The ScPex13p SH3 domain exposes two distinct binding sites for Pex5p and Pex14p

被引：55

作者：

Pires, JR

Hong, XJ

Brockmann, C

Volkmer-Engert, R

Schneider-Mergener, J

Oschkinat, H

Erdmann, R ^{[1
]}

机构：

[1] Ruhr Univ Bochum, Inst Physiol Chem, Fak Med, D-44780 Bochum, Germany

[2] Forschungsinst Mol & Pharmakol, D-13125 Berlin, Germany

[3] Humboldt Univ, Univ Klinikum Charite, Inst Med Immunol, D-10115 Berlin, Germany

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2003年 / 326卷 / 05期

关键词：

SH3; domain; PEX13; PEX5; peroxin; peroxisome;

D O I：

10.1016/S0022-2836(03)00039-1

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：

Pex13p is an essential component of the peroxisomal protein import machinery and interacts via its C-terminal SH3 domain with the type 11 SH3-ligand Pex14p and the non-PXXP protein Pex5p. We report the solution structure of the SH3 domain of Pex13p from Saccharomyces cerevisiae and the identification of a novel-binding pocket, which binds a non-PXXP-peptide representing the binding site of Pex5p. Chemical shift assays revealed the binding sites for Pex5p and Pexl4p ligand peptides to be distinct and spatially separated. Competition assays demonstrated that the two ligand peptides can bind simultaneously to the SH3 domain. (C) 2003 Elsevier Science Ltd. All rights reserved.

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页码：1427 / 1435

页数：9

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