Structural diversity of the hagfish variable lymphocyte receptors

Min Kim Ho, Cheol Oh Se, Jung Lim Ki, Jun Kasamatsu, Young Heo Jin, Seok Park Beom, Hayyoung Lee, Joon Yoo Ook, Masanori Kasahara, Jie Oh Lee

Research output: Contribution to journalArticle

87 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)6726-6732
Number of pages7
JournalJournal of Biological Chemistry
Volume282
Issue number9
DOIs
Publication statusPublished - 2007 Mar 2

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Structural diversity of the hagfish variable lymphocyte receptors'. Together they form a unique fingerprint.

  • Cite this

    Ho, M. K., Se, C. O., Ki, J. L., Kasamatsu, J., Jin, Y. H., Beom, S. P., Lee, H., Ook, J. Y., Kasahara, M., & Lee, J. O. (2007). Structural diversity of the hagfish variable lymphocyte receptors. Journal of Biological Chemistry, 282(9), 6726-6732. https://doi.org/10.1074/jbc.M608471200