| First Author | Min X | Year | 2012 |
| Journal | FEBS Lett | Volume | 586 |
| Issue | 6 | Pages | 912-7 |
| PubMed ID | 22449980 | Mgi Jnum | J:182355 |
| Mgi Id | MGI:5315311 | Doi | 10.1016/j.febslet.2012.02.024 |
| Citation | Min X, et al. (2012) Crystal structure of a single-chain trimer of human adiponectin globular domain. FEBS Lett 586(6):912-7 |
| abstractText | 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 2.0A resolution. The structure reveals a similar trimeric topology to that of mouse gAd protein. Trimer formation is further rigidified by three calcium ions. |
