1sn1: Difference between revisions

New page: left|200px<br /><applet load="1sn1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sn1, resolution 1.7Å" /> '''STRUCTURE OF SCORPION...
 
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[[Image:1sn1.jpg|left|200px]]<br /><applet load="1sn1" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1sn1.jpg|left|200px]]<br /><applet load="1sn1" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1sn1, resolution 1.7&Aring;" />
caption="1sn1, resolution 1.7&Aring;" />
'''STRUCTURE OF SCORPION NEUROTOXIN BMK M1'''<br />
'''STRUCTURE OF SCORPION NEUROTOXIN BMK M1'''<br />


==Overview==
==Overview==
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.
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 Structure==
==About this Structure==
1SN1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mesobuthus_martensii Mesobuthus martensii]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SN1 OCA].  
1SN1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mesobuthus_martensii Mesobuthus martensii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SN1 OCA].  


==Reference==
==Reference==
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[[Category: Mesobuthus martensii]]
[[Category: Mesobuthus martensii]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: He, X.L.]]
[[Category: He, X L.]]
[[Category: Li, H.M.]]
[[Category: Li, H M.]]
[[Category: Liu, X.Q.]]
[[Category: Liu, X Q.]]
[[Category: Wang, D.C.]]
[[Category: Wang, D C.]]
[[Category: Zeng, Z.H.]]
[[Category: Zeng, Z H.]]
[[Category: neurotoxin]]
[[Category: neurotoxin]]
[[Category: scorpion]]
[[Category: scorpion]]
[[Category: sodium channel inhibitor]]
[[Category: sodium channel inhibitor]]


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