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

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,... 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:
Subjects:
Cho
Peg
ID: ISSN: 0014-5793 ; E-ISSN: 1873-3468 ; DOI: 10.1016/j.febslet.2012.02.024
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recordid: wj10.1016/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:
  • Acrp30
  • Adipocyte Complement-Related Protein Of 30 Kda
  • Ampk
  • 5′-Amp-Activated Protein Kinase
  • Cho
  • Chinese Hamster Ovary
  • Peg
  • Polyethylene Glycol
  • Ob/Ob
  • Obese Mouse
  • X-Ray Crystal Structure
  • Adiponectin
  • Single-Chain Globular Domain
  • Calcium Binding
ispartof: FEBS Letters, 23 March 2012, Vol.586(6), pp.912-917
description: 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. ► 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.
language:
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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subjectAcrp30 ; Adipocyte Complement-Related Protein Of 30 Kda ; Ampk ; 5′-Amp-Activated Protein Kinase ; Cho ; Chinese Hamster Ovary ; Peg ; Polyethylene Glycol ; Ob/Ob ; Obese Mouse ; X-Ray Crystal Structure ; Adiponectin ; Single-Chain Globular Domain ; Calcium Binding
descriptionAdiponectin 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. ► 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.
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titleCrystal structure of a single‐chain trimer of human adiponectin globular domain
descriptionAdiponectin 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. ► 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.
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titleCrystal structure of a single‐chain trimer of human adiponectin globular domain
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abstractAdiponectin 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. ► 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.
doi10.1016/j.febslet.2012.02.024
pages912-917
date2012-03-23