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
收藏
页码：411 / 416
页数：6
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