Three-dimensional structure of Selenocosmia huwena lectin-I (SHL-I) from the venom of the spider Selenocosmia huwena by 2D-NMR.
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.
Lü
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National Laboratory of Protein Engineering and Plant Genetic Engineering, Peking University, Beijing, China.
Liang
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Gu
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D000595:Amino Acid Sequence; D019476:Insect Proteins; D037102:Lectins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D013111:Spider Venoms / Q000737:chemistry*
D019476:Insect Proteins; D037102:Lectins; D013111:Spider Venoms; C098229:lectin-like peptide-I, Selenocosmia huwena