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• W2283351635 abstract "Antibodies have been a remarkably successful class of molecules for binding a large number of antigens in therapeutic, diagnostic, and research applications. Typical antibodies derived from mouse or human sources use the surface formed by complementarity determining regions (CDRs) on the variable regions of the heavy chain/light chain heterodimer, which typically forms a relatively flat binding surface. Alternative species, particularly camelids and bovines, provide a unique paradigm for antigen recognition through novel domains which form the antigen binding paratope. For camelids, heavy chain antibodies bind antigen with only a single heavy chain variable region, in the absence of light chains. In bovines, ultralong CDR-H3 regions form an independently folding minidomain, which protrudes from the surface of the antibody and is diverse in both its sequence and disulfide patterns. The atypical paratopes of camelids and bovines potentially provide the ability to interact with different epitopes, particularly recessed or concave surfaces, compared to traditional antibodies." @default.
• W2283351635 created "2016-06-24" @default.
• W2283351635 creator A5016430611 @default.
• W2283351635 creator A5023971009 @default.
• W2283351635 date "2016-06-01" @default.
• W2283351635 modified "2023-10-03" @default.
• W2283351635 title "Distinct antibody species: structural differences creating therapeutic opportunities" @default.
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• W2283351635 doi "https://doi.org/10.1016/j.coi.2016.02.003" @default.
• W2283351635 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4884505" @default.
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• W2283351635 hasPublicationYear "2016" @default.
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