Binding diversity of the two binding sites of ricin B lectin

✍ Scribed by Debabani Ganguly; Chaitali Mukhopadhyay

• Publisher: Wiley (John Wiley & Sons)
• Year: 2006
• Tongue: English
• Weight: 427 KB
• Volume: 83
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.20530

✦ Synopsis

Abstract

Ricin B is a galactose‐binding protein, which contains two binding sites. We have compared the binding properties of the two binding sites of ricin B chain toward different mono‐ and disaccharide ligands. The free energies of binding are calculated using the free energy perturbation simulation (thermodynamic integration method) and linear interaction energy approach using CHARMM force field. The second binding site of the protein was found to be weaker compared to the first. The details of the hydrogen‐bonding scheme suggested the origin of the epimeric specificity of the protein. The reason for the weaker binding capacity of the second binding site has been addressed. © 2006 Wiley Periodicals, Inc. Biopolymers 83: 83–94, 2006

This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at [email protected]