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

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• 作者：Xiaoshan Min^a ; Bryan Lemon^b ; Jie Tang^b ; Qiang Liu^b ; Richard Zhang^b ; Nigel Walker^a ; Yang Li^c ; Zhulun Wang^a ; ^{zwang@amgen.com}
• 关键词：ACRP30 ; adipocyte complement-related protein of 30  ; kDa ; AMPK ; 5&prime ; -AMP-activated protein kinase ; CHO ; Chinese hamster ovary ; PEG ; polyethylene glycol ; ob/ob ; obese mouse
• 刊名：FEBS Letters
• 出版年：2012
• 出版时间：23 March, 2012
• 年：2012
• 卷：586
• 期：6
• 页码：912-917
• 全文大小：1202 K

文摘

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 ? resolution. The structure reveals a similar trimeric topology to that of mouse gAd protein. Trimer formation is further rigidified by three calcium ions.