1I1J
STRUCTURE OF MELANOMA INHIBITORY ACTIVITY PROTEIN: A MEMBER OF A NEW FAMILY OF SECRETED PROTEINS
1I1J の概要
エントリーDOI | 10.2210/pdb1i1j/pdb |
分子名称 | MELANOMA DERIVED GROWTH REGULATORY PROTEIN (2 entities in total) |
機能のキーワード | sh3 subdomain, hormone-growth factor complex, hormone/growth factor |
由来する生物種 | Homo sapiens (human) |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 24516.28 |
構造登録者 | Lougheed, J.C.,Holton, J.M.,Alber, T.,Bazan, J.F.,Handel, T.M. (登録日: 2001-02-02, 公開日: 2001-05-16, 最終更新日: 2011-07-13) |
主引用文献 | Lougheed, J.C.,Holton, J.M.,Alber, T.,Bazan, J.F.,Handel, T.M. Structure of melanoma inhibitory activity protein, a member of a recently identified family of secreted proteins. Proc.Natl.Acad.Sci.USA, 98:5515-5520, 2001 Cited by PubMed Abstract: Melanoma inhibitory activity (MIA) is a 12-kDa protein that is secreted from both chondrocytes and malignant melanoma cells. MIA has been reported to have effects on cell growth and adhesion, and it may play a role in melanoma metastasis and cartilage development. We report the 1.4-A crystal structure of human MIA, which consists of an Src homology 3 (SH3)-like domain with N- and C-terminal extensions of about 20 aa. each. The N- and C-terminal extensions add additional structural elements to the SH3 domain, forming a previously undescribed fold. MIA is a representative of a recently identified family of proteins and is the first structure of a secreted protein with an SH3 subdomain. The structure also suggests a likely protein interaction site and suggests that, unlike conventional SH3 domains, MIA does not recognize polyproline helices. PubMed: 11331761DOI: 10.1073/pnas.091601698 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.39 Å) |
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