3M18
Crystal structure of variable lymphocyte receptor VLRA.R2.1 in complex with hen egg lysozyme
Summary for 3M18
| Entry DOI | 10.2210/pdb3m18/pdb |
| Related | 3M19 |
| Descriptor | Variable lymphocyte receptor A diversity region, Lysozyme C, PHOSPHATE ION, ... (4 entities in total) |
| Functional Keywords | variable lymphocyte receptor, adaptive immunity, antibody, t cell, b cell, leucine-rich repeat, immune system |
| Biological source | Petromyzon marinus (marine lamprey) More |
| Cellular location | Secreted: P00698 |
| Total number of polymer chains | 2 |
| Total formula weight | 41892.04 |
| Authors | Deng, L.,Velikovsky, C.A.,Mariuzza, R.A. (deposition date: 2010-03-04, release date: 2010-06-30, Last modification date: 2024-10-09) |
| Primary citation | Deng, L.,Velikovsky, C.A.,Xu, G.,Iyer, L.M.,Tasumi, S.,Kerzic, M.C.,Flajnik, M.F.,Aravind, L.,Pancer, Z.,Mariuzza, R.A. A structural basis for antigen recognition by the T cell-like lymphocytes of sea lamprey. Proc.Natl.Acad.Sci.USA, 107:13408-13413, 2010 Cited by PubMed Abstract: Adaptive immunity in jawless vertebrates is mediated by leucine-rich repeat proteins called "variable lymphocyte receptors" (VLRs). Two types of VLR (A and B) are expressed by mutually exclusive lymphocyte populations in lamprey. VLRB lymphocytes resemble the B cells of jawed vertebrates; VLRA lymphocytes are similar to T cells. We determined the structure of a high-affinity VLRA isolated from lamprey immunized with hen egg white lysozyme (HEL) in unbound and antigen-bound forms. The VLRA-HEL complex demonstrates that certain VLRAs, like gammadelta T-cell receptors (TCRs) but unlike alphabeta TCRs, can recognize antigens directly, without a requirement for processing or antigen-presenting molecules. Thus, these VLRAs feature the nanomolar affinities of antibodies, the direct recognition of unprocessed antigens of both antibodies and gammadelta TCRs, and the exclusive expression on the lymphocyte surface that is unique to alphabeta and gammadelta TCRs. PubMed: 20616002DOI: 10.1073/pnas.1005475107 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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