1SQ2
Crystal Structure Analysis of the Nurse Shark New Antigen Receptor (NAR) Variable Domain in Complex With Lysozyme
Summary for 1SQ2
| Entry DOI | 10.2210/pdb1sq2/pdb |
| Descriptor | Lysozyme C, novel antigen receptor, CHLORIDE ION, ... (5 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 | 2 |
| Total formula weight | 26732.20 |
| Authors | Stanfield, R.L.,Dooley, H.,Flajnik, M.F.,Wilson, I.A. (deposition date: 2004-03-17, release date: 2004-08-24, Last modification date: 2024-10-09) |
| 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 Cited by 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: 15319492DOI: 10.1126/science.1101148 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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