Human melanoma inhibitory protein binds to the FN12-14 Hep II domain of fibronectin

Biointerphases
King Tuo YipRaphael Stoll

Abstract

The heparin binding site (Hep II) of fibronectin plays a major role in tumor cell metastasis. Its interaction with heparan sulfate proteoglycans occurs in a variety of physiological processes including focal adhesion and migration. The melanoma inhibitory activity (MIA) is an important protein that is functionally involved in melanoma development, progression, and tumor cell invasion. After its secretion by malignant melanoma cells, MIA interacts with fibronectin and thereby actively facilitates focal cell detachment from surrounding structures and strongly promotes tumor cell invasion and the formation of metastases. In this report, the authors have determined the molecular basis of the interaction of MIA with the Hep II domain of fibronectin based on nuclear magnetic resonance spectroscopic binding assays. The authors have identified the type III modules 12 to 14 of fibronectin's Hep II as the major MIA binding sites. These results now provide a new target protein-protein binding interface for the discovery of novel antimetastatic agents against malignant melanoma in the future.

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Citations

Jun 30, 2017·Biointerphases·Tobias Weidner

Related Concepts

MIA protein, human
Protein Domain
Fibronectins
Melanoma
Neoplasm Proteins
Plasma Protein Binding Capacity
Extracellular Matrix Proteins
Protein NMR Spectroscopy
Molecular Docking Analysis
Fibronectins

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