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Science 13 March 1992:
Vol. 255. no. 5050, pp. 1419 - 1421
DOI: 10.1126/science.1542789

Articles

Science, Vol 255, Issue 5050, 1419-1421
Copyright © 1992 by American Association for the Advancement of Science


articles

Long-range attraction and molecular rearrangements in receptor-ligand interactions

DE Leckband, JN Israelachvili, FJ Schmitt, and W Knoll

Department of Chemical and Nuclear Engineering, University of California, Santa Barbara 93106.

A surface force apparatus was used to measure a long-range attractive protein-ligand force at separations D less than 85 angstroms. This force may effectively "steer" ligand trajectories, resulting in a greater than 27-fold enhancement of the association rate. A much stronger specific attraction is measured at contact (D less than 4 angstroms). A sevenfold increase in intermembrane adhesion resulted from increased lateral mobility of the receptors and molecular rearrangements in membranes above the solid-fluid transition temperature.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Neural Cell Adhesion Molecule (N-CAM) Homophilic Binding Mediated by the Two N-terminal Ig Domains Is Influenced by Intramolecular Domain-Domain Interactions.
A. R. Atkins, W. J. Gallin, G. C. Owens, G. M. Edelman, and B. A. Cunningham (2004)
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Designing Human m1 Muscarinic Receptor-Targeted Hydrophobic Eigenmode Matched Peptides as Functional Modulators.
K. A. Selz, A. J. Mandell, M. F. Shlesinger, V. Arcuragi, and M. J. Owens (2004)
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Binding strength between cell adhesion proteoglycans measured by atomic force microscopy.
U Dammer, O Popescu, P Wagner, D Anselmetti, H. Guntherodt, and G. Misevic (1995)
Science 267, 1173-1175
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