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• W2078361457 endingPage "2909" @default.
• W2078361457 startingPage "2901" @default.
• W2078361457 abstract "The new antigen receptor (IgNAR) antibodies from sharks are disulphide bonded dimers of two protein chains, each containing one variable and five constant domains. Three types of IgNAR variable domains have been discovered, with Type 3 appearing early in shark development and being overtaken by the antigen-driven affinity-matured Type 1 and 2 response. Here, we have determined the first structure of a naturally occurring Type 2 IgNAR variable domain, and identified the disulphide bond that links and stabilizes the CDR1 and CDR3 loops. This disulphide bridge locks the CDR3 loop in an “upright” conformation in contrast to other shark antibody structures, where a more lateral configuration is observed. Further, we sought to model the Type 3 isotype based on the crystallographic structure reported here. This modeling indicates (1) that internal Type 3-specific residues combine to pack into a compact immunoglobulin core that supports the CDR loop regions, and (2) that despite apparent low-sequence variability, there is sufficient plasticity in the CDR3 loop to form a conformationally diverse antigen-binding surface." @default.
• W2078361457 created "2016-06-24" @default.
• W2078361457 creator A5029765749 @default.
• W2078361457 creator A5059104878 @default.
• W2078361457 creator A5083111142 @default.
• W2078361457 date "2005-11-01" @default.
• W2078361457 modified "2023-10-16" @default.
• W2078361457 title "Structure of a shark IgNAR antibody variable domain and modeling of an early-developmental isotype" @default.
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• W2078361457 doi "https://doi.org/10.1110/ps.051709505" @default.
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• W2078361457 hasPublicationYear "2005" @default.
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