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- W2108049244 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." @default.
- W2108049244 created "2016-06-24" @default.
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- W2108049244 date "1992-11-01" @default.
- W2108049244 modified "2023-10-16" @default.
- W2108049244 title "The three-dimensional structure of the tenth type III module of fibronectin: An insight into RGD-mediated interactions" @default.
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- W2108049244 doi "https://doi.org/10.1016/0092-8674(92)90600-h" @default.
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