Publication Abstract from PubMed
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.
Structure of melanoma inhibitory activity protein, a member of a recently identified family of secreted proteins.,Lougheed JC, Holton JM, Alber T, Bazan JF, Handel TM Proc Natl Acad Sci U S A. 2001 May 8;98(10):5515-20. Epub 2001 May 1. PMID:11331761[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
