The solution structure of the SODD BAG domain reveals additional electrostatic interactions in the HSP70 complexes of SODD subfamily BAG domains

被引：10

作者：

Brockmann, C

Leitner, D

Labudde, D

Diehl, A

Sievert, V

Büssow, K

Kühne, R

Oschkinat, H

机构：

[1] Forschungsinst Mol Pharmakol, D-13125 Berlin, Germany

[2] Free Univ Berlin, D-1000 Berlin, Germany

[3] Max Planck Inst Mol Genet, Berlin, Germany

来源：

FEBS LETTERS | 2004年 / 558卷 / 1-3期

关键词：

silencer of death domains; Bcl-associated athanogene 4; heat shock protein 70; nuclear magnetic resonance structure; homology model;

D O I：

10.1016/S0014-5793(03)01490-X

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：

The solution structure of an N-terminally extended construct of the SODD BAG domain was determined by nuclear magnetic resonance spectroscopy. A homology model of the SODD-BAG/HSP70 complex reveals additional possible interactions that are specific for the SODD subfamily of BAG domains while the overall geometry of the complex remains the same. Relaxation rate measurements show that amino acids N358-S375 of SODD which were previously assigned to its BAG domain are not structured in our construct. The SODD BAG domain is thus indeed smaller than the homologous domain in Bag1 defining a new subfamily of BAG domains. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：101 / 106

页数：6

共 30 条

[1] Isolation of Bcl-2 binding proteins that exhibit homology with BAG-1 and suppressor of death domains protein [J].