title: Structure of melanoma inhibitory activity protein, a member of a recently identified family of secreted proteins.
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.
authors.affiliation: Department of Molecular and Cell Biology, 229 Stanley Hall, University of California, Berkeley, CA 94720, USA.
authors.forename: J C
authors.initials: JC
authors.lastname: Lougheed
authors.forename: J M
authors.initials: JM
authors.lastname: Holton
authors.forename: T
authors.initials: T
authors.lastname: Alber
authors.forename: J F
authors.initials: JF
authors.lastname: Bazan
authors.forename: T M
authors.initials: TM
authors.lastname: Handel
mesh_terms: D000595:Amino Acid Sequence; D016326:Extracellular Matrix Proteins; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins / Q000737:chemistry*; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
chemical_list: D016326:Extracellular Matrix Proteins; C090059:MIA protein, human; D009363:Neoplasm Proteins