1t6v | pdb_00001t6v
Crystal structure analysis of the nurse shark new antigen receptor (NAR) variable domain in complex with lysozyme
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| 1t6v, resolution 1.70Å | |||||||||||||
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| Ligands: | CL | ||||||||||||
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
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.
About this Structure
1T6V is a Protein complex structure of sequences from Gallus gallus and Ginglymostoma cirratum. Full crystallographic information is available from OCA.
Reference
Crystal structure of a shark single-domain antibody V region in complex with lysozyme., Stanfield RL, Dooley H, Flajnik MF, Wilson IA, Science. 2004 Sep 17;305(5691):1770-3. Epub 2004 Aug 19. PMID:15319492
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