3E6J

Crystal Structure of Variable Lymphocyte Receptor (VLR) RBC36 in Complex with H-trisaccharide

3E6J の概要

• エントリーDOI: 10.2210/pdb3e6j/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900036
• 分子名称: Variable lymphocyte receptor diversity region, alpha-L-fucopyranose-(1-2)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: variable lymphocyte receptors, vlr, leucine-rich repeat, lrr, adaptive immunity, immune system, sea lamprey, jawless fish, receptor
• 由来する生物種: Petromyzon marinus (marine lamprey)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26321.67

構造登録者

Han, B.W.,Herrin, B.R.,Cooper, M.D.,Wilson, I.A. (登録日: 2008-08-15, 公開日: 2008-10-07, 最終更新日: 2024-11-20)

主引用文献

Han, B.W.,Herrin, B.R.,Cooper, M.D.,Wilson, I.A.
Antigen recognition by variable lymphocyte receptors.
Science, 321:1834-1837, 2008

PubMed Abstract: Variable lymphocyte receptors (VLRs) rather than antibodies play the primary role in recognition of antigens in the adaptive immune system of jawless vertebrates. Combinatorial assembly of leucine-rich repeat (LRR) gene segments achieves the required repertoire for antigen recognition. We have determined a crystal structure for a VLR-antigen complex, VLR RBC36 in complex with the H-antigen trisaccharide from human blood type O erythrocytes, at 1.67 angstrom resolution. RBC36 binds the H-trisaccharide on the concave surface of the LRR modules of the solenoid structure where three key hydrophilic residues, multiple van der Waals interactions, and the highly variable insert of the carboxyl-terminal LRR module determine antigen recognition and specificity. The concave surface assembled from the most highly variable regions of the LRRs, along with diversity in the sequence and length of the highly variable insert, can account for the recognition of diverse antigens by VLRs.

PubMed: 18818359
DOI: 10.1126/science.1162484

実験手法

X-RAY DIFFRACTION (1.67 Å)