title: The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions.
abstract: The solution structure of the tenth type III module of fibronectin has been determined using nuclear magnetic resonance techniques. The molecule has a fold similar to that of immunoglobulin domains, with seven beta strands forming two antiparallel beta sheets, which pack against each other. Both beta 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.
authors.affiliation: Department of Biochemistry, University of Oxford, England.
authors.forename: A L
authors.initials: AL
authors.lastname: Main
authors.forename: T S
authors.initials: TS
authors.lastname: Harvey
authors.forename: M
authors.initials: M
authors.lastname: Baron
authors.forename: J
authors.initials: J
authors.lastname: Boyd
authors.forename: I D
authors.initials: ID
authors.lastname: Campbell
mesh_terms: D000595:Amino Acid Sequence; D005353:Fibronectins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D011971:Receptors, Immunologic / Q000737:chemistry*
chemical_list: D005353:Fibronectins; D009842:Oligopeptides; D011971:Receptors, Immunologic; C047981:arginyl-glycyl-aspartic acid