2o6r
From Proteopedia
Structural diversity of the hagfish Variable Lymphocyte Receptors B61
Overview
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.
About this Structure
2O6R is a Single protein structure of sequence from Eptatretus burgeri. Full crystallographic information is available from OCA.
Reference
Structural diversity of the hagfish variable lymphocyte receptors., Kim HM, Oh SC, Lim KJ, Kasamatsu J, Heo JY, Park BS, Lee H, Yoo OJ, Kasahara M, Lee JO, J Biol Chem. 2007 Mar 2;282(9):6726-32. Epub 2006 Dec 27. PMID:17192264 Page seeded by OCA on Sun May 4 10:23:50 2008
