Add time:08/24/2019         Source:sciencedirect.com

The solution structure of the tenth type III module of fibronectin has been determined using nuclear magetic resonance techniques. The molecule has a fold similar to that of immunoglobulin domains, with seven β strands forming two antiparallel β sheets, which pack against each other. Both β sheets contribute conserved hydrophobic residues to a compact core. The topology is more similar to that of domain 2 of CD4, PapD, and the extracellular domain of the human growth hormone receptor than to that of immunoglobulin C domains. The module contains an Arg-Gly-Asp sequence known to be involved in cell adhesion. This tripeptide is solvent exposed and lies on a conformationally mobile loop between strands F and G, consistent with its cell adhesion function.

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