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Published Online August 19, 2004
Science DOI: 10.1126/science.1101148

Reports

Submitted on June 7, 2004
Accepted on August 4, 2004

Crystal Structure of a Shark Single-Domain Antibody V Region in Complex with Lysozyme

Robyn L. Stanfield 1, Helen Dooley 2, Martin F. Flajnik 2, Ian A. Wilson 3*

1 Department of Molecular Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, CA 92037, USA.
2 Department of Microbiology and Immunology, University of Maryland at Baltimore, Baltimore, MD 21201-1559, USA.
3 Department of Molecular Biology and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, CA 92037, USA.

* To whom correspondence should be addressed.
Ian A. Wilson , E-mail: wilson{at}scripps.edu

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 (IgNAR) in which the variable domains recognize antigen with only a single Ig domain, akin to camelid VHH domains. The 1.45 Å resolution crystal structure of the Type I IgNAR variable 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 (CDRs), but still binds HEL with nanomolar affinity via a binding interface comparable in size to conventional antibodies.


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Science. ISSN 0036-8075 (print), 1095-9203 (online)