Crystal structure of the PB1 domain of NBR1

被引：17

作者：

Müller, S ^{[1
]}

Kursula, I ^{[1
]}

Zou, P ^{[1
]}

Wilmanns, M ^{[1
]}

机构：

[1] DESY, EMBL Hamburg Outstn, D-22603 Hamburg, Germany

来源：

FEBS LETTERS | 2006年 / 580卷 / 01期

关键词：

PB1; domain; titin; signal transduction; X-ray crystallography;

D O I：

10.1016/j.febslet.2005.12.021

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 scaffold protein NBR1 is involved in signal transmission downstream of the serine/protein kinase from the giant muscle protein titin. Its N-terminal Phox and Bem1p (PB1) domain plays a critical role in mediating protein-protein interactions with both titin kinase and with another scaffold protein, p62. We have determined the crystal structure of the PB1 domain of NBR1 at 1.55 angstrom resolution. It reveals a type-A PB1 domain with two negatively charged residue clusters. We provide a structural perspective on the involvement of NBR1 in the titin kinase signalling pathway. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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页码：341 / 344

页数：4

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