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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Min X,Lemon B,Tang J,Liu Q,Zhang R,Walker N,Li Y,Wang Zdoi
10.1016/j.febslet.2012.02.024subject
Has Abstractpub_date
2012-03-23 00:00:00pages
912-7issue
6eissn
0014-5793issn
1873-3468pii
S0014-5793(12)00133-0journal_volume
586pub_type
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