1hjd
From Proteopedia
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MELANOMA INHIBITORY ACTIVITY (MIA) PROTEIN
Contents |
Overview
Melanoma inhibitory activity (MIA) protein is a clinically valuable marker, in patients with malignant melanoma, as enhanced values diagnose, metastatic melanoma stages III and IV. Here we show that the recombinant, human MIA adopts an SH3 domain-like fold in solution, with two, perpendicular, antiparallel, three- and five-stranded beta-sheets. In, contrast to known structures with the SH3 domain fold, MIA is a, single-domain protein, and contains an additional antiparallel beta-sheet, and two disulfide bonds. MIA is also the first extracellular protein found, to have the SH3 domain-like fold. Furthermore, we show that MIA interacts, with fibronectin and that the peptide ligands identified for MIA exhibit a, matching sequence to type III human fibronectin repeats, especially to, FN14, which is close to an integrin alpha4beta1 binding site. The present, study, therefore, may explain the role of MIA in metastasis in vivo, and, supports a model in which the binding of human MIA to type III repeats of, fibronectin competes with integrin binding, thus detaching cells from the, extracellular matrix.
Disease
Known disease associated with this structure: Myocardial infarction, susceptibility to OMIM:[611082]
About this Structure
1HJD is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The extracellular human melanoma inhibitory activity (MIA) protein adopts an SH3 domain-like fold., Stoll R, Renner C, Zweckstetter M, Bruggert M, Ambrosius D, Palme S, Engh RA, Golob M, Breibach I, Buettner R, Voelter W, Holak TA, Bosserhoff AK, EMBO J. 2001 Feb 1;20(3):340-9. PMID:11157741
Page seeded by OCA on Fri Feb 15 15:56:54 2008
