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

Altroff, H., Schlinkert, R., Walle, C.F., Bernini, A., Campbell, I.D., Werner, J.M. and Mardon, H.J. (2004) Interdomain tilt angle determines integrin-dependent function of the ninth and tenth FIII domains of human fibronectin The Journal of Biological Chemistry, 279, (53), pp. 55995-56003. (doi:10.1074/jbc.M406976200).

Record type: 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 51 and v3 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 51 binding and downstream function. The precise molecular basis of this synergy remains elusive. Here we have dissected further the function of FIII9 in integrin binding by analyzing the biological activity of the FIII9-10 interdomain interface variants and by determining their structural and dynamic properties in solution. We demonstrate that the contribution of FIII9 to both 51 and v3 binding and downstream function critically depends upon the interdomain tilt between the FIII9 and FIII10 domains. Our data suggest that modulation of integrin binding by FIII9 may arise in part from its steric properties that determine accessibility of the RGD motif. These findings have wider implications for mechanisms of integrin-ligand binding in the physiological context.

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Published date: 1 December 2004


Local EPrints ID: 56743
ISSN: 0021-9258
PURE UUID: e5b3c04d-8d7a-443a-b97c-cce504675977
ORCID for J.M. Werner: ORCID iD

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Date deposited: 07 Aug 2008
Last modified: 17 Jul 2017 14:30

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Author: H. Altroff
Author: R. Schlinkert
Author: C.F. Walle
Author: A. Bernini
Author: I.D. Campbell
Author: J.M. Werner ORCID iD
Author: H.J. Mardon

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