1t6v
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(New page: 200px<br /> <applet load="1t6v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t6v, resolution 1.70Å" /> '''Crystal structure a...)
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Revision as of 07:35, 18 November 2007
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Crystal structure analysis of the nurse shark new antigen receptor (NAR) variable domain in complex with lysozyme
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 with CL as ligand. Active as Lysozyme, with EC number 3.2.1.17 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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