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1sn1

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{{STRUCTURE_1sn1| PDB=1sn1 | SCENE= }}
{{STRUCTURE_1sn1| PDB=1sn1 | SCENE= }}
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'''STRUCTURE OF SCORPION NEUROTOXIN BMK M1'''
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===STRUCTURE OF SCORPION NEUROTOXIN BMK M1===
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==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Scorpion]]
[[Category: Scorpion]]
[[Category: Sodium channel inhibitor]]
[[Category: Sodium channel inhibitor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:58:42 2008''

Revision as of 10:58, 28 July 2008

Image:1sn1.png

Template:STRUCTURE 1sn1

STRUCTURE OF SCORPION NEUROTOXIN BMK M1

Template:ABSTRACT PUBMED 10493862

About this Structure

1SN1 is a Single protein structure of sequence from Mesobuthus martensii. Full crystallographic information is available from OCA.

Reference

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

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