{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Spurrier B"],"funding":["NIAID NIH HHS","NHLBI NIH HHS","NIGMS NIH HHS"],"pagination":["691-9"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3096878"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["19(5)"],"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 Ab"],"journal":["Structure (London, England : 1993)"],"pubmed_title":["Structural analysis of human and macaque mAbs 2909 and 2.5B: implications for the configuration of the quaternary neutralizing epitope of HIV-1 gp120."],"pmcid":["PMC3096878"],"funding_grant_id":["AI036085","AI082274","GM088118","P30 AI027742","R01 AI036085","R01 AI084119","T32 GM088118","AI077451","HL059725","P01 AI082274","R01 HL059725","AI084119","R21 AI077451","AI027742"],"pubmed_authors":["Sampson JM","Li H","Kong XP","Robinson J","O'Neal T","Gorny MK","Totrov M","Williams C","Zolla-Pazner S","Spurrier B"],"additional_accession":[]},"is_claimable":false,"name":"Structural analysis of human and macaque mAbs 2909 and 2.5B: implications for the configuration of the quaternary neutralizing epitope of HIV-1 gp120.","description":"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 Ab","dates":{"release":"2011-01-01T00:00:00Z","publication":"2011 May","modification":"2026-04-15T23:26:00.032Z","creation":"2026-04-07T14:04:50.759Z"},"accession":"S-EPMC3096878","cross_references":{"pubmed":["21565703"],"doi":["10.1016/j.str.2011.02.012"]}}