Cell
Volume 71, Issue 4, 13 November 1992, Pages 671-678
Journal home page for Cell

Article
The three-dimensional structure of the tenth type III module of fibronectin: An insight into RGD-mediated interactions

https://doi.org/10.1016/0092-8674(92)90600-HGet rights and content

Abstract

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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    Present address: Boyer Center for Molecular Medicine, Yale University School of Medicine, 295 Congress Avenue, New Haven, Connecticut 06536.

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