Structure of Rhamnose-binding Lectin CSL3: Unique Pseudo-tetrameric Architecture of a Pattern Recognition Protein

Tsuyoshi Shirai, Yasuharu Watanabe, Min sub Lee, Tomohisa Ogawa, Koji Muramoto

Research output: Contribution to journalArticlepeer-review

40 Citations (Scopus)

Abstract

The crystal structure of the l-rhamnose-binding lectin CSL3 was determined to 1.8 Å resolution. This protein is a component of the germline-encoded pattern recognition proteins in innate immunity. CSL3 is a homodimer of two 20 kDa subunits with a dumbbell-like shape overall, in which the N- and C-terminal domains of different subunits form lobe structures connected with flexible linker peptides. The complex structures of the protein with specific carbohydrates demonstrated the importance of the most variable loop region among homologues for the specificity toward oligosaccharides. CSL3 and Shiga-like toxin both use Gb3 as a cellular receptor to evoke apoptosis. They have very different overall architecture but share the separation distance between carbohydrate-binding sites. An inspection of the structure database suggested that the pseudo-tetrameric structure of CSL3 was unique among the known lectins. This architecture implies this protein might provide a unique tool for further investigations into the relationships between architecture and function of pattern recognition proteins.

Original languageEnglish
Pages (from-to)390-403
Number of pages14
JournalJournal of Molecular Biology
Volume391
Issue number2
DOIs
Publication statusPublished - 2009 Aug 14

Keywords

  • X-ray crystallography
  • bioinformatics
  • globotriose
  • innate immunity
  • lectin

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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