1T6V

Crystal structure analysis of the nurse shark new antigen receptor (NAR) variable domain in complex with lysozyme

Summary for 1T6V

• Entry DOI: 10.2210/pdb1t6v/pdb
• Related: 1SQ2
• Descriptor: Lysozyme C, novel antigen receptor, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: immunoglobulin fold, protein-protein complex, hydrolase-immune system complex, hydrolase/immune system
• Biological source: Ginglymostoma cirratum (nurse shark); More
• Cellular location: Secreted: P00698
• Total number of polymer chains: 4
• Total formula weight: 52843.72

Authors

Stanfield, R.L.,Dooley, H.,Flajnik, M.F.,Wilson, I.A. (deposition date: 2004-05-07, release date: 2004-08-24, Last modification date: 2024-11-20)

Primary citation

Stanfield, R.L.,Dooley, H.,Flajnik, M.F.,Wilson, I.A.
Crystal structure of a shark single-domain antibody V region in complex with lysozyme.
Science, 305:1770-1773, 2004

PubMed Abstract: 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.

PubMed: 15319492
DOI: 10.1126/science.1101148

Experimental method

X-RAY DIFFRACTION (1.7 Å)