The structure of an FF domain from human HYPA/FBP11
The structure of an FF domain from human HYPA/FBP11
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DOI：
10.1016/s0022-2836(02)00968-3
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发表时间：
2002-10-25
影响因子：
5.6
通讯作者：
Bycroft, M
中科院分区：
文献类型：
--
作者：
Allen, M;Friedler, A;Bycroft, M
Ff结构域是一个60个氨基酸残基的磷酸肽结合模块，存在于多种真核蛋白中，包括转录延伸因子CA150、剪接因子Prp40和p190RHOGAP。我们已经从HYPA/FBP11中确定了FF域的结构。结构域由三个a螺旋组成，排列成正交束，在第二个和第三个a螺旋之间的环中有一个3(10)螺旋。该结构不同于其他磷肽结合域的结构，代表了一种新的磷肽结合折叠。(C)2002爱思唯尔科学有限公司。保留所有权利。
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.