2O6Q

Structural diversity of the hagfish Variable Lymphocyte Receptors A29

Summary for 2O6Q

• Entry DOI: 10.2210/pdb2o6q/pdb
• Related: 2O6R 2O6S
• Descriptor: Variable lymphocyte receptor A (2 entities in total)
• Functional Keywords: leucine-rich repeat protein, lrr, immune system
• Biological source: Eptatretus burgeri (inshore hagfish)
• Total number of polymer chains: 1
• Total formula weight: 30137.84

Authors

Lee, J.O.,Kim, H.M.,Oh, S.C. (deposition date: 2006-12-08, release date: 2006-12-26, Last modification date: 2024-11-20)

Primary citation

Kim, H.M.,Oh, S.C.,Lim, K.J.,Kasamatsu, J.,Heo, J.Y.,Park, B.S.,Lee, H.,Yoo, O.J.,Kasahara, M.,Lee, J.O.
Structural diversity of the hagfish variable lymphocyte receptors
J.Biol.Chem., 282:6726-6732, 2007

PubMed Abstract: Variable lymphocyte receptors (VLRs) are recently discovered leucine-rich repeat (LRR) family proteins that mediate adaptive immune responses in jawless fish. Phylogenetically it is the oldest adaptive immune receptor and the first one with a non-immunoglobulin fold. We present the crystal structures of one VLR-A and two VLR-B clones from the inshore hagfish. The hagfish VLRs have the characteristic horseshoe-shaped structure of LRR family proteins. The backbone structures of their LRR modules are highly homologous, and the sequence variation is concentrated on the concave surface of the protein. The conservation of key residues suggests that our structures are likely to represent the LRR structures of the entire repertoire of jawless fish VLRs. The analysis of sequence variability, prediction of protein interaction surfaces, amino acid composition analysis, and structural comparison with other LRR proteins suggest that the hypervariable concave surface is the most probable antigen binding site of the VLR.

PubMed: 17192264
DOI: 10.1074/jbc.M608471200

Experimental method

X-RAY DIFFRACTION (2.5 Å)