{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Clark KR"],"funding":["NIAID NIH HHS","National Institutes of Health"],"pagination":["2429-41"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2821263"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["18(12)"],"pubmed_abstract":["We present the crystal structure determination of an anti-HIV-1 gp120 single-chain variable fragment antibody variant, 3B3, at 2.5 A resolution. This 3B3 variant was derived from the b12 antibody, using phage display and site-directed mutagenesis of the variable heavy chain (V(H)) complementary-determining regions (CDRs). 3B3 exhibits enhanced binding affinity and neutralization activity against several cross-clade primary isolates of HIV-1 by interaction with the recessed CD4-binding site on the gp120 envelope protein. Comparison with the structures of the unbound and bound forms of b12, the 3B3 structure closely resembles these structures with minimal differences with two notable exceptions. First, there is a reorientation of the CDR-H3 of the V(H) domain where the primary sequences evol"],"journal":["Protein science : a publication of the Protein Society"],"pubmed_title":["Crystal structure of a 3B3 variant--a broadly neutralizing HIV-1 scFv antibody."],"pmcid":["PMC2821263"],"funding_grant_id":["P01 AI056354"],"pubmed_authors":["Walsh ST","Clark KR"],"additional_accession":[]},"is_claimable":false,"name":"Crystal structure of a 3B3 variant--a broadly neutralizing HIV-1 scFv antibody.","description":"We present the crystal structure determination of an anti-HIV-1 gp120 single-chain variable fragment antibody variant, 3B3, at 2.5 A resolution. This 3B3 variant was derived from the b12 antibody, using phage display and site-directed mutagenesis of the variable heavy chain (V(H)) complementary-determining regions (CDRs). 3B3 exhibits enhanced binding affinity and neutralization activity against several cross-clade primary isolates of HIV-1 by interaction with the recessed CD4-binding site on the gp120 envelope protein. Comparison with the structures of the unbound and bound forms of b12, the 3B3 structure closely resembles these structures with minimal differences with two notable exceptions. First, there is a reorientation of the CDR-H3 of the V(H) domain where the primary sequences evol","dates":{"release":"2009-01-01T00:00:00Z","publication":"2009 Dec","modification":"2025-06-01T02:30:09.865Z","creation":"2019-03-26T22:31:56Z"},"accession":"S-EPMC2821263","cross_references":{"pubmed":["19785005"],"doi":["10.1002/pro.255"]}}