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bioRxivBiochemistry

On-rate modulation of cadherin interactions by chemical fragments

A. Senoo, S. Ito, S. Nagatoishi, Y. Saito, G. Ueno, K. Yoshida, T. Tashima, S. Kudo, S. Sando, K. Tsumoto

PDFDOIPreprint

Abstract

Many cadherin family proteins are associated with diseases such as cancer. Since cell adhesion requires homodimerization of cadherin molecules, a small-molecule regulator of dimerization would have therapeutic potential. Herein, we describe identification of a P-cadherin-specific chemical fragment that inhibits P-cadherin-mediated cell adhesion. Although the identified molecule is a fragment compound, it binds to a cavity of P-cadherin that has not previously been targeted, indirectly prevents formation of hydrogen bonds necessary for formation of an intermediate called the X dimer and thus modulates the on-rate of X dimerization. Our findings will impact on a strategy for kinetic regulation of protein-protein interactions and stepwise assembly of protein complexes using small molecules.

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