Molecular model for the complex between Concanavalin A and a biantennary-complex class glycopeptide

✍ Scribed by J. P. Carver; A. E. MacKenzie; K. D. Hardman

• Publisher: Wiley (John Wiley & Sons)
• Year: 1985
• Tongue: English
• Weight: 915 KB
• Volume: 24
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.360240106

✦ Synopsis

A molecular model for the complex formed between the jack bean lectin concanavalin A (Con A) and glycopeptides of the complex biantennary class is described. The model was derived using coordinate: for Con A determined by x-ray crystallographic refinement techniques, with 1.75-A resolution data, and coordinates for the glycopeptides obtained from 'H-nmr measurements, using the nuclear Overhauser effect. Previous solution and crystallographic studies provided several constraints on the possible mode of interaction of the lectin and the glycopeptide. Examination of the model suggests that the glycopeptide binding site is defined by four loops on the protein surface made up by amino acid residues: 12-18,98-102,205-208, and 226-229. Within these loops, it has been possible to identify the sidechain and backbone atoms responsible for the favorable interactions with high-affinity ligands and those responsible for the unfavorable interactions with poor ligands.