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'''STRUCTURE OF MELANOMA INHIBITORY ACTIVITY PROTEIN: A MEMBER OF A NEW FAMILY OF SECRETED PROTEINS''' | '''STRUCTURE OF MELANOMA INHIBITORY ACTIVITY PROTEIN: A MEMBER OF A NEW FAMILY OF SECRETED PROTEINS''' | ||
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[[Category: Holton, J M.]] | [[Category: Holton, J M.]] | ||
[[Category: Lougheed, J C.]] | [[Category: Lougheed, J C.]] | ||
[[Category: | [[Category: Sh3 subdomain]] | ||
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Revision as of 16:27, 2 May 2008
STRUCTURE OF MELANOMA INHIBITORY ACTIVITY PROTEIN: A MEMBER OF A NEW FAMILY OF SECRETED PROTEINS
Overview
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.
About this Structure
1I1J is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 19:27:54 2008
