{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Stewart A"],"funding":["NIAID NIH HHS","NIGMS NIH HHS"],"pagination":["9"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3626704"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14"],"pubmed_abstract":["<h4>Background</h4>Analysis of factors contributing to high affinity antibody-protein interactions provides insight into natural antibody evolution, and guides the design of antibodies with new or enhanced function. We previously studied the interaction between antibody D5 and its target, a designed protein based on HIV-1 gp41 known as 5-Helix, as a model system [Da Silva, G. F.; Harrison, J. S.; Lai, J. R., Biochemistry, 2010, 49, 5464-5472]. Antibody D5 represents an interesting case study because it is derived from the VH1-69 germline segment; this germline segment is characterized by a hydrophobic second heavy chain complementarity determining region (HCDR2) that constitutes the major functional paratope in D5 and several antibodies derived from the same progenitor.<h4>Results</h4>Here"],"journal":["BMC biochemistry"],"pubmed_title":["Side chain requirements for affinity and specificity in D5, an HIV-1 antibody derived from the VH1-69 germline segment."],"pmcid":["PMC3626704"],"funding_grant_id":["P30-AI51519","R01-AI090249","T32-GM008572","R01 AI090249"],"pubmed_authors":["Regula LK","Lai JR","Harrison JS","Stewart A"],"additional_accession":[]},"is_claimable":false,"name":"Side chain requirements for affinity and specificity in D5, an HIV-1 antibody derived from the VH1-69 germline segment.","description":"<h4>Background</h4>Analysis of factors contributing to high affinity antibody-protein interactions provides insight into natural antibody evolution, and guides the design of antibodies with new or enhanced function. We previously studied the interaction between antibody D5 and its target, a designed protein based on HIV-1 gp41 known as 5-Helix, as a model system [Da Silva, G. F.; Harrison, J. S.; Lai, J. R., Biochemistry, 2010, 49, 5464-5472]. Antibody D5 represents an interesting case study because it is derived from the VH1-69 germline segment; this germline segment is characterized by a hydrophobic second heavy chain complementarity determining region (HCDR2) that constitutes the major functional paratope in D5 and several antibodies derived from the same progenitor.<h4>Results</h4>Here","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Apr","modification":"2025-04-04T11:48:02.065Z","creation":"2019-03-27T01:07:26Z"},"accession":"S-EPMC3626704","cross_references":{"pubmed":["23566198"],"doi":["10.1186/1471-2091-14-9"]}}