Structures of HIV-1 gp120 envelope glycoproteins from laboratory-adapted and primary isolates.
Kwong, P.D., Wyatt, R., Majeed, S., Robinson, J., Sweet, R.W., Sodroski, J., Hendrickson, W.A.(2000) Structure 8: 1329-1339
- PubMed: 11188697 
- DOI: https://doi.org/10.1016/s0969-2126(00)00547-5
- Primary Citation of Related Structures:  
1G9M, 1G9N - PubMed Abstract: 
The gp120 exterior envelope glycoprotein of HIV-1 binds sequentially to CD4 and chemokine receptors on cells to initiate virus entry. During natural infection, gp120 is a primary target of the humoral immune response, and it has evolved to resist antibody-mediated neutralization. We previously reported the structure at 2.5 A of a gp120 core from the HXBc2 laboratory-adapted isolate in complex with a 2 domain fragment of CD4 and the antigen binding fragment of a human antibody. This revealed atomic details of gp120-receptor interactions and suggested multiple mechanisms of immune evasion.
Organizational Affiliation: 
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032, USA.