The structural basis for the recognition of diverse receptor sequences by TRAF2

被引：242

作者：

Ye, H

Park, YC

Kreishman, M

Kieff, E

Wu, H ^{[1
]}

机构：

[1] Cornell Univ, Dept Biochem, Weill Med Coll, New York, NY 10021 USA

[2] Cornell Univ, Grad Sch Med Sci, New York, NY 10021 USA

[3] Harvard Univ, Sch Med, Dept Med, Dept Microbiol & Mol Genet, Boston, MA 02115 USA

来源：

MOLECULAR CELL | 1999年 / 4卷 / 03期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/S1097-2765(00)80334-2

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：

Many members of the tumor necrosis factor receptor (TNFR) superfamily initiate intracellular signaling by recruiting TNFR-associated factors (TRAFs) through their cytoplasmic tails. TRAFs apparently recognize highly diverse receptor sequences. crystal structures of the TRAF domain of human TRAF2 in complex with peptides from the TNFR family members CD40, CD30, Ox40, 4-1BB, and the EBV oncoprotein LMP1 revealed a conserved binding mode. A major TRAF2-binding consensus sequence, (P/S/A/T)x(Q/E)E, and a minor consensus motif, PxQxxD, can be defined from the structural analysis, which encompass all known TRAF2-binding sequences. The structural information provides a template for the further dissection of receptor binding specificity of TRAF2 and for the understanding of the complexity of TRAF-mediated signal transduction.

引用

收藏

页码：321 / 330

页数：10

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