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3M18

Crystal structure of variable lymphocyte receptor VLRA.R2.1 in complex with hen egg lysozyme

Summary for 3M18
Entry DOI10.2210/pdb3m18/pdb
Related3M19
DescriptorVariable lymphocyte receptor A diversity region, Lysozyme C, PHOSPHATE ION, ... (4 entities in total)
Functional Keywordsvariable lymphocyte receptor, adaptive immunity, antibody, t cell, b cell, leucine-rich repeat, immune system
Biological sourcePetromyzon marinus (marine lamprey)
More
Cellular locationSecreted: P00698
Total number of polymer chains2
Total formula weight41892.04
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 citationDeng, 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: 20616002
DOI: 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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