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Publication Abstract from PubMed

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.

Three-dimensional structure of Selenocosmia huwena lectin-I (SHL-I) from the venom of the spider Selenocosmia huwena by 2D-NMR.,Lu S, Liang S, Gu X J Protein Chem. 1999 Jul;18(5):609-17. PMID:10524779^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.