The structure of an FF domain from human HYPA/FBP11

被引：78

作者：

Allen, M ^{[1
]}

Friedler, A ^{[1
]}

Schon, O ^{[1
]}

Bycroft, M ^{[1
]}

机构：

[1] MRC, Ctr Prot Engn, Cambridge CB2 2QH, England

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2002年 / 323卷 / 03期

关键词：

NMR structure; transcription; phosphopeptide recognition; RNA polymerase II carboxyl-terminal domain;

D O I：

10.1016/S0022-2836(02)00968-3

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 FF domain is a 60 amino acid residue phosphopeptide-binding module found in a variety of eukaryotic proteins including the transcription elongation factor CA150, the splicing factor Prp40 and p190RHOGAP. We have determined the structure of an FF domain from HYPA/FBP11. The domain is composed of three a helices arranged in an orthogonal bundle with a 3(10) helix in the loop between the second and third a helices. The structure differs from those of other phosphopeptide-binding domains and represents a novel phosphopeptide-binding fold. (C) 2002 Elsevier Science Ltd. All rights reserved.

引用

页码：411 / 416

页数：6

共 23 条

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