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1: Science. 2004 Sep 17;305(5691):1770-3. Epub 2004 Aug 19.Click here to read Links

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

Stanfield RL, Dooley H, Flajnik MF, Wilson IA.

Department of Molecular Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.

Cartilaginous fish are the phylogenetically 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.

PMID: 15319492 [PubMed - indexed for MEDLINE]

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