1i1j
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(New page: 200px<br /> <applet load="1i1j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i1j, resolution 1.39Å" /> '''STRUCTURE OF MELANO...)
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Revision as of 15:18, 12 November 2007
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STRUCTURE OF MELANOMA INHIBITORY ACTIVITY PROTEIN: A MEMBER OF A NEW FAMILY OF SECRETED PROTEINS
Contents |
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.
Disease
Known disease associated with this structure: Myocardial infarction, susceptibility to OMIM:[611082]
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
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