Crystal structure of a shark single-domain antibody V region in complex with lysozyme

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Abstract

Cartilaginous fish are the phytogenetically oldest living organisms known to possess components of the vertebrate adaptive immune system. Key to their immune response are heavy-chain, homodimeric immunoglobulins called new antigen receptors (IgNARs), in which the variable (V) domains recognize antigens with only a single immunoglobulin domain, akin to camelid heavy-chain V domains. The 1.45 angstrom resolution crystal structure of the type I IgNAR V domain in complex with hen egg-white lysozyme (HEL) reveals a minimal antigen-binding domain that contains only two of the three conventional complementarity- determining regions but still binds HEL with nanomolar affinity by means of a binding interface comparable in size to conventional antibodies.

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Stanfield, R. L., Dooley, H., Flajnik, M. F., & Wilson, I. A. (2004). Crystal structure of a shark single-domain antibody V region in complex with lysozyme. Science, 305(5691), 1770–1773. https://doi.org/10.1126/science.1101148

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