Solution Structure of a Cyanovirin-N:Man alpha 1-2Man alpha Complex. Structural Basis for High Affinity Carbohydrate-Mediated Binding to gp120
Bewley, C.A.(2001) Structure 9: 931-940
- PubMed: 11591348 
- DOI: https://doi.org/10.1016/s0969-2126(01)00653-0
- Primary Citation of Related Structures:  
1IIY - PubMed Abstract: 
Cyanovirin-N (CVN) is a novel, 11 kDa cyanobacterial protein that potently inhibits viral entry by diverse strains of HIV through high-affinity carbohydrate-mediated interactions with the viral envelope glycoprotein gp120. CVN contains two symmetry-related carbohydrate binding sites of differing affinities that selectively bind to Man(8) D1D3 and Man(9) with nanomolar affinities, the carbohydrates that also mediate CVN:gp120 binding. High-resolution structural studies of CVN in complex with a representative oligosaccharide are desirable for understanding the structural basis for this unprecedented specificity.
Organizational Affiliation: 
Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA. caroleb@intra.niddk.nih.gov