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{{STRUCTURE_1sn1| PDB=1sn1 | SCENE= }} | |||
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'''STRUCTURE OF SCORPION NEUROTOXIN BMK M1''' | '''STRUCTURE OF SCORPION NEUROTOXIN BMK M1''' | ||
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[[Category: Wang, D C.]] | [[Category: Wang, D C.]] | ||
[[Category: Zeng, Z H.]] | [[Category: Zeng, Z H.]] | ||
[[Category: | [[Category: Neurotoxin]] | ||
[[Category: | [[Category: Scorpion]] | ||
[[Category: | [[Category: Sodium channel inhibitor]] | ||
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Revision as of 08:54, 3 May 2008
STRUCTURE OF SCORPION NEUROTOXIN BMK M1
OverviewOverview
The crystal structures of two group III alpha-like toxins from the scorpion Buthus martensii Karsch, BmK M1 and BmK M4, were determined at 1.7 A and 1.3 A resolution and refined to R factors of 0.169 and 0.166, respectively. The first high-resolution structures of the alpha-like scorpion toxin show some striking features compared with structures of the "classical" alpha-toxin. Firstly, a non-proline cis peptide bond between residues 9 and 10 unusually occurs in the five-member reverse turn 8-12. Secondly, the cis peptide 9-10 mediates the spatial relationship between the turn 8-12 and the C-terminal stretch 58-64 through a pair of main-chain hydrogen bonds between residues 10 and 64 to form a unique tertiary arrangement which features the special orientation of the terminal residues 62-64. Finally, in consequence of the peculiar orientation of the C-terminal residues, the functional groups of Arg58, which are crucial for the toxin-receptor interaction, are exposed and accessible in BmK M1 and M4 rather than buried as in the classical alpha-toxins. Sequence alignment and characteristics analysis suggested that the above structural features observed in BmK M1 and M4 occur in all group III alpha-like toxins. Recently, some group III alpha-like toxins were demonstrated to occupy a receptor site different from the classical alpha-toxin. Therefore, the distinct structural features of BmK M1 and M4 presented here may provide the structural basis for the newly recognized toxin-receptor binding site selectivity. Besides, the non-proline cis peptide bonds found in these two structures play a role in the formation of the structural characteristics and in keeping accurate positions of the functionally crucial residues. This manifested a way to achieve high levels of molecular specificity and atomic precision through the strained backbone geometry.
About this StructureAbout this Structure
1SN1 is a Single protein structure of sequence from Mesobuthus martensii. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of two alpha-like scorpion toxins: non-proline cis peptide bonds and implications for new binding site selectivity on the sodium channel., He XL, Li HM, Zeng ZH, Liu XQ, Wang M, Wang DC, J Mol Biol. 1999 Sep 10;292(1):125-35. PMID:10493862 Page seeded by OCA on Sat May 3 08:54:33 2008