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1i1j
From Proteopedia
| 1i1j, resolution 1.39Å () | |||||||||||
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| Domains: | SH3_2 | ||||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||
STRUCTURE OF MELANOMA INHIBITORY ACTIVITY PROTEIN: A MEMBER OF A NEW FAMILY OF SECRETED PROTEINS
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1I1J is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Lougheed JC, Holton JM, Alber T, Bazan JF, Handel TM. Structure of melanoma inhibitory activity protein, a member of a recently identified family of secreted proteins. Proc Natl Acad Sci U S A. 2001 May 8;98(10):5515-20. Epub 2001 May 1. PMID:11331761 doi:10.1073/pnas.091601698
Page seeded by OCA on Tue Feb 17 02:42:54 2009
