Structural highlights
Function
Q9YK84_9HEPC
Publication Abstract from PubMed
We have determined the crystal structure of broadly neutralizing antibody (bnAb) AP33 bound to a peptide corresponding to hepatitis C virus (HCV) E2 envelope glycoprotein antigenic site 412-423. Comparison with bnAb HCV1 bound to the same epitope reveals a different angle of approach to the antigen by bnAb AP33, and slight variation in its beta-hairpin conformation of the epitope. These structures establish two different modes of binding to E2 that antibodies adopt to neutralize diverse HCV.
Structure of hepatitis C virus envelope glycoprotein E2 antigenic site 412-423 in complex with antibody AP33.,Kong L, Giang E, Nieusma T, Robbins JB, Deller MC, Stanfield RL, Wilson IA, Law M J Virol. 2012 Sep 12. PMID:22973046[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kong L, Giang E, Nieusma T, Robbins JB, Deller MC, Stanfield RL, Wilson IA, Law M. Structure of hepatitis C virus envelope glycoprotein E2 antigenic site 412-423 in complex with antibody AP33. J Virol. 2012 Sep 12. PMID:22973046 doi:http://dx.doi.org/10.1128/JVI.01939-12