{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Jenkins GW"],"funding":["NICHD NIH HHS","HHS | NIH | National Institute of General Medical Sciences","HHS | NIH | Eunice Kennedy Shriver National Institute of Child Health and Human Development","NIGMS NIH HHS"],"pagination":["2141-2148"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9940733"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["209(11)"],"pubmed_abstract":["Ab \"ultralong\" third H chain complementarity-determining regions (CDR H3) appear unique to bovine Abs and may enable binding to difficult epitopes that shorter CDR H3 regions cannot easily access. Diversity is concentrated in the \"knob\" domain of the CDR H3, which is encoded by the DH gene segment and sits atop a β-ribbon \"stalk\" that protrudes far from the Ab surface. Knob region cysteine content is quite diverse in terms of total number of cysteines, sequence position, and disulfide bond pattern formation. We investigated the role of germline cysteines in production of a diverse CDR H3 structural repertoire. The relationship between DH polymorphisms and deletions relative to germline at the nucleotide level, as well as diversity in cysteine and disulfide bond content at the structural le"],"journal":["Journal of immunology (Baltimore, Md. : 1950)"],"pubmed_title":["Germline-Encoded Positional Cysteine Polymorphisms Enhance Diversity in Antibody Ultralong CDR H3 Regions."],"pmcid":["PMC9940733"],"funding_grant_id":["R01GM105826","R01 HD088400","R01HD088400","R01 GM105826"],"pubmed_authors":["Smider VV","Jenkins GW","Safonova Y"],"additional_accession":[]},"is_claimable":false,"name":"Germline-Encoded Positional Cysteine Polymorphisms Enhance Diversity in Antibody Ultralong CDR H3 Regions.","description":"Ab \"ultralong\" third H chain complementarity-determining regions (CDR H3) appear unique to bovine Abs and may enable binding to difficult epitopes that shorter CDR H3 regions cannot easily access. Diversity is concentrated in the \"knob\" domain of the CDR H3, which is encoded by the DH gene segment and sits atop a β-ribbon \"stalk\" that protrudes far from the Ab surface. Knob region cysteine content is quite diverse in terms of total number of cysteines, sequence position, and disulfide bond pattern formation. We investigated the role of germline cysteines in production of a diverse CDR H3 structural repertoire. The relationship between DH polymorphisms and deletions relative to germline at the nucleotide level, as well as diversity in cysteine and disulfide bond content at the structural le","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Dec","modification":"2026-05-29T07:38:02.509Z","creation":"2025-02-19T01:16:44.321Z"},"accession":"S-EPMC9940733","cross_references":{"pubmed":["36426974"],"doi":["10.4049/jimmunol.2200455"]}}