Glycosylation assists binding of HIV protein gp120 to human CD4 receptor

Dennis Wilhelm; Henning N Behnken; Bernd Meyer

doi:10.1002/cbic.201100740

Glycosylation assists binding of HIV protein gp120 to human CD4 receptor

Chembiochem. 2012 Mar 5;13(4):524-7. doi: 10.1002/cbic.201100740. Epub 2012 Jan 20.

Authors

Dennis Wilhelm¹, Henning N Behnken, Bernd Meyer

Affiliation

¹ Organic Chemistry, University of Hamburg, Martin-Luther-King-Platz 6, 20146 Hamburg, Germany.

PMID: 22266649
DOI: 10.1002/cbic.201100740

Abstract

The role of glycosylation of proteins on its binding affinity is not well understood. Even a monosaccharide (magenta) placed at a glycosylation site can significantly enhance binding of peptides to their receptor. If glycosylated, an HIV protein binds stronger and faster to its primary receptors on human cells.

Publication types

Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Binding Sites
CD4 Antigens / chemistry*
CD4 Antigens / metabolism*
Glycosylation
HIV Envelope Protein gp120 / chemistry*
HIV Envelope Protein gp120 / metabolism*
Humans
Models, Molecular
Molecular Conformation
Molecular Sequence Data

Substances

CD4 Antigens
HIV Envelope Protein gp120