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

► We solved the structure of a single-chain trimer of human adiponectiin globular domain. ► The structure revealed a trimeric topology similar to other C1q family proteins. ► The trimeric formation is rigidified by three intrinsic calcium ions. Adiponectin is increasingly recognized as a potential t... Full description

Journal Title: FEBS Letters 23 March 2012, Vol.586(6), pp.912-917
Main Author: Min, Xiaoshan
Other Authors: Lemon, Bryan , Tang, Jie , Liu, Qiang , Zhang, Richard , Walker, Nigel , Li, Yang , Wang, Zhulun
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0014-5793 ; E-ISSN: 1873-3468 ; DOI: 10.1016/j.febslet.2012.02.024
Link: https://www.sciencedirect.com/science/article/pii/S0014579312001330
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recordid: elsevier_sdoi_10_1016_j_febslet_2012_02_024
title: Crystal structure of a single-chain trimer of human adiponectin globular domain
format: Article
creator:
  • Min, Xiaoshan
  • Lemon, Bryan
  • Tang, Jie
  • Liu, Qiang
  • Zhang, Richard
  • Walker, Nigel
  • Li, Yang
  • Wang, Zhulun
subjects:
  • X-Ray Crystal Structure
  • Adiponectin
  • Single-Chain Globular Domain
  • Calcium Binding
  • Biology
  • Chemistry
  • Anatomy & Physiology
ispartof: FEBS Letters, 23 March 2012, Vol.586(6), pp.912-917
description: ► We solved the structure of a single-chain trimer of human adiponectiin globular domain. ► The structure revealed a trimeric topology similar to other C1q family proteins. ► The trimeric formation is rigidified by three intrinsic calcium ions. 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 Å resolution. The structure reveals a similar trimeric topology to that of mouse gAd protein. Trimer formation is further rigidified by three calcium ions.
language: eng
source:
identifier: ISSN: 0014-5793 ; E-ISSN: 1873-3468 ; DOI: 10.1016/j.febslet.2012.02.024
fulltext: fulltext
issn:
  • 0014-5793
  • 00145793
  • 1873-3468
  • 18733468
url: Link


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titleCrystal structure of a single-chain trimer of human adiponectin globular domain
creatorMin, Xiaoshan ; Lemon, Bryan ; Tang, Jie ; Liu, Qiang ; Zhang, Richard ; Walker, Nigel ; Li, Yang ; Wang, Zhulun
ispartofFEBS Letters, 23 March 2012, Vol.586(6), pp.912-917
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subjectX-Ray Crystal Structure ; Adiponectin ; Single-Chain Globular Domain ; Calcium Binding ; Biology ; Chemistry ; Anatomy & Physiology
description► We solved the structure of a single-chain trimer of human adiponectiin globular domain. ► The structure revealed a trimeric topology similar to other C1q family proteins. ► The trimeric formation is rigidified by three intrinsic calcium ions. 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 Å resolution. The structure reveals a similar trimeric topology to that of mouse gAd protein. Trimer formation is further rigidified by three calcium ions.
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