title: Crystal structure of a single-chain trimer of human adiponectin globular domain.
abstract: 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 2.0Å resolution. The structure reveals a similar trimeric topology to that of mouse gAd protein. Trimer formation is further rigidified by three calcium ions.
authors.affiliation: Department of Molecular Structure, Amgen Inc., South San Francisco, CA 94080, USA.
authors.forename: Xiaoshan
authors.initials: X
authors.lastname: Min
authors.forename: Bryan
authors.initials: B
authors.lastname: Lemon
authors.forename: Jie
authors.initials: J
authors.lastname: Tang
authors.forename: Qiang
authors.initials: Q
authors.lastname: Liu
authors.forename: Richard
authors.initials: R
authors.lastname: Zhang
authors.forename: Nigel
authors.initials: N
authors.lastname: Walker
authors.forename: Yang
authors.initials: Y
authors.lastname: Li
authors.forename: Zhulun
authors.initials: Z
authors.lastname: Wang
mesh_terms: D052242:Adiponectin / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D000818:Animals; D002118:Calcium / Q000378:metabolism; D018360:Crystallography, X-Ray; D006801:Humans; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
chemical_list: C499918:ADIPOQ protein, human; D052242:Adiponectin; D011994:Recombinant Proteins; D002118:Calcium