Ligand binding analysis for human alpha5beta1 integrin: strategies for designing new alpha5beta1 integrin antagonists.

Luciana Marinelli, Axel Meyer, Dominik Heckmann, Antonio Lavecchia, Ettore Novellino, Horst Kessler

Journal: Journal of medicinal chemistry 2005;48(13):4204-7

PMID: 15974570

Full Text on American Chemical Society View on PubMed

Abstract

We report a three-dimensional model of the alpha5beta1 integrin headgroup bound to the most potent and selective ligand (SJ749) known to date. The model was built using the comparative protein modeling method, and it is consistent with experimental data. From this study, we identified two potentially important regions in the alpha5beta1 receptor that are peculiar to this integrin and might be worth considering for drug targeting.

Address: Dipartimento di Chimica Farmaceutica e Tossicologica, Università di Napoli Federico II, Via D. Montesano, 49-80131 Napoli, Italy.

DOI: 10.1021/jm040224i

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https://doi.org/10.1021/jm040224i

MeSH Terms: Amino Acid Sequence, Binding Sites, Drug Design, Humans, Imidazoles, Integrin alpha5beta1, Ligands, Peptide Fragments, Protein Conformation, Protein Subunits, Sequence Alignment