2O6Q

Structural diversity of the hagfish Variable Lymphocyte Receptors A29

2O6Q の概要

• エントリーDOI: 10.2210/pdb2o6q/pdb
• 関連するPDBエントリー: 2O6R 2O6S
• 分子名称: Variable lymphocyte receptor A (2 entities in total)
• 機能のキーワード: leucine-rich repeat protein, lrr, immune system
• 由来する生物種: Eptatretus burgeri (inshore hagfish)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30137.84

構造登録者

Lee, J.O.,Kim, H.M.,Oh, S.C. (登録日: 2006-12-08, 公開日: 2006-12-26, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.5 Å)