3Q6G

Crystal structure of Fab of rhesus mAb 2.5B specific for quaternary neutralizing epitope of HIV-1 gp120

Summary for 3Q6G

• Entry DOI: 10.2210/pdb3q6g/pdb
• Related: 3Q6F
• Descriptor: Light chain of Fab of rhesus mAb 2.5B, Heavy chain of Fab of rhesus mAb 2.5B (3 entities in total)
• Functional Keywords: ig, neutralization of hiv-1 viruses, quaternary epitope of hiv-1 gp120, immune system
• Biological source: Macaca mulatta (Rhesus monkey); More
• Total number of polymer chains: 4
• Total formula weight: 93921.52

Authors

Spurrier, B.,Sampson, J.,Totrov, M.,Li, H.,O'Neal, T.,William, C.,Robinson, J.,Gorny, M.K.,Zolla-Pazner, S.,Kong, X.P. (deposition date: 2010-12-31, release date: 2011-05-25, Last modification date: 2024-10-30)

Primary citation

Spurrier, B.,Sampson, J.M.,Totrov, M.,Li, H.,O'Neal, T.,Williams, C.,Robinson, J.,Gorny, M.K.,Zolla-Pazner, S.,Kong, X.P.
Structural Analysis of Human and Macaque mAbs 2909 and 2.5B: Implications for the Configuration of the Quaternary Neutralizing Epitope of HIV-1 gp120.
Structure, 19:691-699, 2011

PubMed Abstract: The quaternary neutralizing epitope (QNE) of HIV-1 gp120 is preferentially expressed on the trimeric envelope spikes of intact HIV virions, and QNE-specific monoclonal antibodies (mAbs) potently neutralize HIV-1. Here, we present the crystal structures of the Fabs of human mAb 2909 and macaque mAb 2.5B. Both mAbs have long beta hairpin CDR H3 regions >20 Å in length that are each situated at the center of their respective antigen-binding sites. Computational analysis showed that the paratopes include the whole CDR H3, while additional CDR residues form shallow binding pockets. Structural modeling suggests a way to understand the configuration of QNEs and the antigen-antibody interaction for QNE mAbs. Our data will be useful in designing immunogens that may elicit potent neutralizing QNE Abs.

PubMed: 21565703
DOI: 10.1016/j.str.2011.02.012

Experimental method

X-RAY DIFFRACTION (1.902 Å)