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Biophys. J. BioFAST: First Published December 1, 2006. doi:10.1529/biophysj.106.097048
© 2006 by the Biophysical Society.

A more recent version of this article appeared on March 1, 2007.
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BIOPHYSICAL THEORY AND MODELING

A structure-based sliding-rebinding mechanism for catch bonds

Jizhong Lou 1 and Cheng Zhu 1*

1 Georgia Institute of Technology

* To whom correspondence should be addressed. E-mail: cheng.zhu{at}me.gatech.edu.

Submitted on September 7, 2006
Revised on October 26, 2006
Accepted on 10 November 2006


  Abstract
Catch bonds, whose lifetimes are prolonged by force, have been observed in selectin-ligand interactions and other systems. Several biophysical models have been proposed to explain this counter-intuitive phenomenon, but none was based on the structure of the interacting molecules and the noncovalent interactions at the binding interface. Here we used molecular dynamics simulations to study changes in structure and atomic-level interactions during forced unbinding of P-selectin from P-selectin glycoprotein ligand-1. A mechanistic model for catch bonds was developed based on these observations. In the model, "catch" results from forced opening of an interdomain hinge that tilts the binding interface to allow two sides of the contact to slide against each other. Sliding promotes formation of new interactions and even rebinding to the original state, thereby slowing dissociation and prolonging bond lifetimes. Properties of this sliding-rebinding mechanism were explored using a pseudo-atom representation and Monte Carlo simulations. The model has been supported by its ability to fit experimental data and can be related to previously proposed two-pathway models.

Key Words: Catch bonds, kinetics, off-rate, selectin




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Copyright © 2006 by the Biophysical Society.