Crystal structure of a single-chain trimer of human adiponectin globular domain

被引：38
|
作者：
Min, Xiaoshan [1 ]
Lemon, Bryan [2 ]
Tang, Jie [2 ]
Liu, Qiang [2 ]
Zhang, Richard [2 ]
Walker, Nigel [1 ]
Li, Yang [3 ]
Wang, Zhulun [1 ]
机构：
[1] Amgen Inc, Dept Mol Struct, 1120 Vet Blvd, San Francisco, CA 94080 USA
[2] Amgen Inc, Dept Prot Sci, San Francisco, CA 94080 USA
[3] Amgen Inc, Dept Metab Disorders, San Francisco, CA 94080 USA
来源：
FEBS LETTERS | 2012年 / 586卷 / 06期
关键词：
X-ray crystal structure; Adiponectin; Single-chain globular domain; Calcium binding; COMPLEMENT-RELATED PROTEIN; INSULIN-RESISTANCE; ADIPOSE; EXPRESSION; OBESITY; MICE; C1Q;
D O I：
10.1016/j.febslet.2012.02.024
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：
Adiponectin is increasingly recognized as a potential therapeutic agent for the treatment of diabetes and other metabolic diseases. It circulates in plasma as homotrimers and higher-order oliogomers of homotrimers. To facilitate the production of active recombinant adiponectin as a therapeutic tool, we designed a single-chain globular domain adiponectin (sc-gAd) in which three monomer sequences are linked together in tandem to form one contiguous polypeptide. Here, we present the crystal structure of human sc-gAd at 2.0 angstrom resolution. The structure reveals a similar trimeric topology to that of mouse gAd protein. Trimer formation is further rigidified by three calcium ions. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码：912 / 917
页数：6
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