3M19

Crystal structure of variable lymphocyte receptor VLRA.R5.1

Summary for 3M19

• Entry DOI: 10.2210/pdb3m19/pdb
• Related: 3M18
• Descriptor: Variable lymphocyte receptor A diversity region (2 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)
• Total number of polymer chains: 2
• Total formula weight: 54955.93

Authors

Deng, L.,Velikovsky, C.A.,Mariuzza, R.A. (deposition date: 2010-03-04, release date: 2010-06-30, Last modification date: 2024-11-06)

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

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

Experimental method

X-RAY DIFFRACTION (1.7 Å)