A novel RING finger in the C-terminal domain of the coatomer protein α-COP

被引：7
|
作者：
Kaur, Gurmeet [1 ]
Subramanian, Srikrishna [1 ]
机构：
[1] CSIR Inst Microbial Technol IMTECH, Chandigarh 160036, India
来源：
BIOLOGY DIRECT | 2015年 / 10卷
关键词：
Cellular transport; Coat protein; Coated vesicles; Tethering complex; Zinc finger; COATED VESICLES; EPSILON-COP; TM-ALIGN; COMPLEX; TRANSPORT; SUBUNIT; HVPS18; SERVER;
D O I：
10.1186/s13062-015-0099-9
中图分类号：
Q [生物科学];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
The C-terminal domain of alpha-COP, an essential subunit of the COPI coatomer complex, is composed of an all alpha- helical region and a small beta-sheet domain. We show that this beta-sheet domain is a Really Interesting New Gene (RING)-like treble clef zinc finger. The zinc-binding residues are substituted by other aminoacids in many homologs including the structurally-characterized proteins from Saccharomyces cerevisiae and Bos taurus. This RING-like domain is possibly related to those of other vesicle membrane-associated complexes, such as CORVET, HOPS and SEA, and likely mediates interactions with Dsl1p and assist in coat oligomerization.
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页数：6
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