Interdomain tilt angle determines integrin-dependent function of the ninth and tenth FIII domains of human fibronectin.

Journal article

Integrins are an important family of signaling receptors that mediate diverse cellular processes. The binding of the abundant extracellular matrix ligand fibronectin to integrins alpha(5)beta(1) and alpha(v)beta(3) is known to depend upon the Arg-Gly-Asp (RGD) motif on the tenth fibronectin FIII domain. The adjacent ninth FIII domain provides a synergistic effect on RGD-mediated integrin alpha(5)beta(1) binding and downstream function. The precise molecular basis of this synergy remains elusi...

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Authors: Altroff, H; Schlinkert, R; van der Walle, C; Bernini, A; Campbell, I

• Journal: Journal of biological chemistry
• Volume: 279
• Issue: 53
• Pages: 55995-56003
• Publication date: 2004-12-01
• DOI: 10.1074/jbc.m406976200
• EISSN: 1083-351X
• ISSN: 0021-9258
• Language: English
• Keywords: DNA; Cell Adhesion; Dose-Response Relationship, Drug; Integrin alphaVbeta3; Enzyme-Linked Immunosorbent Assay; Thermodynamics; Disulfides; Protein Structure, Tertiary; Amino Acid Motifs; Ligands; Protein Folding; Integrins; Fibronectins; Protein Conformation; Protein Denaturation; Oligopeptides; Humans; Protein Binding; Magnetic Resonance Spectroscopy; Models, Molecular