1I1J

STRUCTURE OF MELANOMA INHIBITORY ACTIVITY PROTEIN: A MEMBER OF A NEW FAMILY OF SECRETED PROTEINS

Summary for 1I1J

• Entry DOI: 10.2210/pdb1i1j/pdb
• Descriptor: MELANOMA DERIVED GROWTH REGULATORY PROTEIN (2 entities in total)
• Functional Keywords: sh3 subdomain, hormone-growth factor complex, hormone/growth factor
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 24516.28

Authors

Lougheed, J.C.,Holton, J.M.,Alber, T.,Bazan, J.F.,Handel, T.M. (deposition date: 2001-02-02, release date: 2001-05-16, Last modification date: 2011-07-13)

Primary citation

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

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: 11331761
DOI: 10.1073/pnas.091601698

Experimental method

X-RAY DIFFRACTION (1.39 Å)