Related Content
Search Google Scholar for:
More Information
Related Jobs from ScienceCareers
|
Originally published in Science Express on 19 August 2004
Science 17 September 2004: Vol. 305. no. 5691, pp. 1770 - 1773
DOI: 10.1126/science.1101148
|
|
Reports
Crystal Structure of a Shark Single-Domain Antibody V Region in Complex with Lysozyme
Robyn L. Stanfield,1*
Helen Dooley,3*
Martin F. Flajnik,3
Ian A. Wilson1,2
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.
1 Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
2 Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
3 Department of Microbiology and Immunology, University of Maryland at Baltimore, Baltimore, MD 212011559, USA, and the National Aquarium in Baltimore, 501 E. Pratt Street, Baltimore, MD 21202, USA.
Note added in proof: While this paper was in production, a paper reporting the structures of the two unliganded type 2 IgNAR variable domains was published (42).
* These authors contributed equally to this work.
To whom correspondence should be addressed. E-mail: wilson{at}scripps.edu
Read the Full Text
THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
- High-affinity lamprey VLRA and VLRB monoclonal antibodies.
- S. Tasumi, C. A. Velikovsky, G. Xu, S. A. Gai, K. D. Wittrup, M. F. Flajnik, R. A. Mariuzza, and Z. Pancer (2009)
PNAS
106, 12891-12896
| Abstract »
| Full Text »
| PDF »
- Engineered Human Antibody Constant Domains with Increased Stability.
- R. Gong, B. K. Vu, Y. Feng, D. A. Prieto, M. A. Dyba, J. D. Walsh, P. Prabakaran, T. D. Veenstra, S. G. Tarasov, R. Ishima, et al. (2009)
J. Biol. Chem.
284, 14203-14210
| Abstract »
| Full Text »
| PDF »
- Aggregation-resistant VHs selected by in vitro evolution tend to have disulfide-bonded loops and acidic isoelectric points.
- M. Arbabi-Ghahroudi, R. To, N. Gaudette, T. Hirama, W. Ding, R. MacKenzie, and J. Tanha (2009)
Protein Eng. Des. Sel.
22, 59-66
| Abstract »
| Full Text »
| PDF »
- Single Variable Domain-IgG Fusion: A NOVEL RECOMBINANT APPROACH TO Fc DOMAIN-CONTAINING BISPECIFIC ANTIBODIES.
- J. Shen, M. D. Vil, X. Jimenez, M. Iacolina, H. Zhang, and Z. Zhu (2006)
J. Biol. Chem.
281, 10706-10714
| Abstract »
| Full Text »
| PDF »
- An evolutionarily mobile antigen receptor variable region gene: Doubly rearranging NAR-TcR genes in sharks.
- M. F. Criscitiello, M. Saltis, and M. F. Flajnik (2006)
PNAS
103, 5036-5041
| Abstract »
| Full Text »
| PDF »
- Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies.
- E. De Genst, K. Silence, K. Decanniere, K. Conrath, R. Loris, J. Kinne, S. Muyldermans, and L. Wyns (2006)
PNAS
103, 4586-4591
| Abstract »
| Full Text »
| PDF »
- First molecular and biochemical analysis of in vivo affinity maturation in an ectothermic vertebrate.
- H. Dooley, R. L. Stanfield, R. A. Brady, and M. F. Flajnik (2006)
PNAS
103, 1846-1851
| Abstract »
| Full Text »
| PDF »
- Structure of a {gamma}{delta} T Cell Receptor in Complex with the Nonclassical MHC T22.
- E. J. Adams, Y.-H. Chien, and K. C. Garcia (2005)
Science
308, 227-231
| Abstract »
| Full Text »
| PDF »
|
|