Work by Paul Mould and others has been published in today’s issue of Biochemical Journal.

Targeting ligand-binding sites in integrins // Image by Adam Byron

This study shows that zebrafish α5 integrins do not bind human fibronectin or human α5β1 antagonists, the latter of which have therapeutic potential as anti-angiogenic agents in cancer and diseases of the eye. Exploiting the ligand-binding features of zebrafish α5 integrin, a gain-of-function mutagenesis approach was used to identify the regions of the α5 subunit required for interactions with human fibronectin ligand or human α5β1 antagonists. These results will aid the development of more potent α5β1 antagonists and of in vivo models suitable for drug screening or discovery.

The article was selected by the journal editors as this issue’s Spotlight paper for the BJ Signal knowledge environment.

The paper was originally published online as a Biochemical Journal Immediate Publication on 14 September 2009.

Citation: AP Mould, EJ Koper, A Byron, G Zahn, MJ Humphries, Mapping the ligand-binding pocket of integrin α5β1 using a gain-of-function approach. Biochem. J. 424, 179–189 (2009). DOI | PubMed