<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Stewart A</submitter><funding>NIAID NIH HHS</funding><funding>NIGMS NIH HHS</funding><pagination>9</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3626704</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>14</volume><pubmed_abstract>&lt;h4>Background&lt;/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.&lt;h4>Results&lt;/h4>Here</pubmed_abstract><journal>BMC biochemistry</journal><pubmed_title>Side chain requirements for affinity and specificity in D5, an HIV-1 antibody derived from the VH1-69 germline segment.</pubmed_title><pmcid>PMC3626704</pmcid><funding_grant_id>P30-AI51519</funding_grant_id><funding_grant_id>R01-AI090249</funding_grant_id><funding_grant_id>T32-GM008572</funding_grant_id><funding_grant_id>R01 AI090249</funding_grant_id><pubmed_authors>Regula LK</pubmed_authors><pubmed_authors>Lai JR</pubmed_authors><pubmed_authors>Harrison JS</pubmed_authors><pubmed_authors>Stewart A</pubmed_authors></additional><is_claimable>false</is_claimable><name>Side chain requirements for affinity and specificity in D5, an HIV-1 antibody derived from the VH1-69 germline segment.</name><description>&lt;h4>Background&lt;/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.&lt;h4>Results&lt;/h4>Here</description><dates><release>2013-01-01T00:00:00Z</release><publication>2013 Apr</publication><modification>2025-04-04T11:48:02.065Z</modification><creation>2019-03-27T01:07:26Z</creation></dates><accession>S-EPMC3626704</accession><cross_references><pubmed>23566198</pubmed><doi>10.1186/1471-2091-14-9</doi></cross_references></HashMap>