Three-dimensional structure of Selenocosmia huwena lectin-I (SHL-I) from the venom of the spider Selenocosmia huwena by 2D-NMR

J Protein Chem. 1999 Jul;18(5):609-17. doi: 10.1023/a:1020663619657.

Abstract

The three-dimensional structure of native SHL-I, a lectin from the venom of the Chinese bird spider Selenocosmia huwena, has been determined from two-dimensional 1H NMR spectroscopy recorded at 500 and 600 MHz. The best 10 structures have NOE violation <0.3 A, dihedral violation <2 deg, and average root-mean-square differences of 0.85 + 0.06 A over backbone atoms. The structure consists of a three-stranded antiparallel beta-sheet and three turns. The three disulfide bridges and three-stranded antiparallel beta-sheet form a inhibitor cystine knot motif which is adopted by several other small proteins, such as huwentoxin-I, omega-conotoxin, and gurmarin. The C-terminal fragment from Leu28 to Trp32 adopts two sets of conformations corresponding to the cis and trans conformations of Pro31. The structure of SHL-I also has high similarity with that of the N-terminus of hevein, a lectin from rubber-tree latex.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Insect Proteins*
  • Lectins / chemistry*
  • Magnetic Resonance Spectroscopy / methods*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Spider Venoms / chemistry*

Substances

  • Insect Proteins
  • Lectins
  • Spider Venoms
  • lectin-like peptide-I, Selenocosmia huwena