1hjd
From Proteopedia
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| - | [[Image:1hjd.jpg|left|200px]] | + | [[Image:1hjd.jpg|left|200px]] |
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| - | '''MELANOMA INHIBITORY ACTIVITY (MIA) PROTEIN''' | + | {{Structure |
| + | |PDB= 1hjd |SIZE=350|CAPTION= <scene name='initialview01'>1hjd</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''MELANOMA INHIBITORY ACTIVITY (MIA) PROTEIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HJD is a [ | + | 1HJD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HJD OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11157741 11157741] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: signal]] | [[Category: signal]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:37:50 2008'' |
Revision as of 09:37, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 11:37:50 2008
