1pvz: Difference between revisions

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[[Image:1pvz.gif|left|200px]]<br /><applet load="1pvz" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1pvz.gif|left|200px]]<br /><applet load="1pvz" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1pvz" />

'''Solution Structure of BmP07, A Novel Potassium Channel Blocker from Scorpion Buthus martensi Karsch, 15 structures'''<br />

==Overview==

A natural K+ channel blocker, BmKK2 (a member of scorpion toxin subfamily, alpha-KTx 14), which is composed of 31 amino acid residues and purified, from the venom of the Chinese scorpion Buthus martensi Karsch, was, characterized using whole-cell patch-clamp recording in rat hippocampal, neurons. The three dimensional structure of BmKK2 was determined with, two-dimensional NMR spectroscopy and molecular modelling techniques. In, solution this toxin adopted a common alpha/beta-motif, but showed distinct, local conformation in the loop between alpha-helix and beta-sheet in, comparison with typical short-chain scorpion toxins (e.g., CTX and NTX)., Also, the alpha helix is shorter and the beta-sheet element is smaller, (each strand consisted only two residues). The unusual structural feature, of BmKK2 was attributed to the shorter loop between the alpha-helix and, beta-sheet and the presence of two consecutive Pro residues at position 21, and 22 in the loop. Moreover, two models of BmKK2/hKv1.3 channel and, BmKK2/rSK2 channel complexes were simulated with docking calculations. The, results demonstrated the existence of a alpha-mode binding between the, toxin and the channels. The model of BmKK2/rSK2 channel complex exhibited, favorable contacts both in electrostatic and hydrophobic, including a, network of five hydrogen bonds and bigger interface containing seven pairs, of inter-residue interactions. In contrast, the model of BmKK2/hKv1.3, channel complex, containing only three pairs of inter-residue, interactions, exhibited poor contacts and smaller interface. The results, well explained its lower activity towards Kv channel, and predicted that, it may prefer a type of SK channel with a narrower entryway as its, specific receptor.

A natural K+ channel blocker, BmKK2 (a member of scorpion toxin subfamily alpha-KTx 14), which is composed of 31 amino acid residues and purified from the venom of the Chinese scorpion Buthus martensi Karsch, was characterized using whole-cell patch-clamp recording in rat hippocampal neurons. The three dimensional structure of BmKK2 was determined with two-dimensional NMR spectroscopy and molecular modelling techniques. In solution this toxin adopted a common alpha/beta-motif, but showed distinct local conformation in the loop between alpha-helix and beta-sheet in comparison with typical short-chain scorpion toxins (e.g., CTX and NTX). Also, the alpha helix is shorter and the beta-sheet element is smaller (each strand consisted only two residues). The unusual structural feature of BmKK2 was attributed to the shorter loop between the alpha-helix and beta-sheet and the presence of two consecutive Pro residues at position 21 and 22 in the loop. Moreover, two models of BmKK2/hKv1.3 channel and BmKK2/rSK2 channel complexes were simulated with docking calculations. The results demonstrated the existence of a alpha-mode binding between the toxin and the channels. The model of BmKK2/rSK2 channel complex exhibited favorable contacts both in electrostatic and hydrophobic, including a network of five hydrogen bonds and bigger interface containing seven pairs of inter-residue interactions. In contrast, the model of BmKK2/hKv1.3 channel complex, containing only three pairs of inter-residue interactions, exhibited poor contacts and smaller interface. The results well explained its lower activity towards Kv channel, and predicted that it may prefer a type of SK channel with a narrower entryway as its specific receptor.

==About this Structure==

1PVZ 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=1PVZ OCA].

1PVZ 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=1PVZ OCA].

==Reference==

Line 22:

[[Category: alpha/beta scaffold]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 00:10:~~23 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:33:05 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1pvz.gif|left|200px]]<br /><applet load="1pvz" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1pvz.gif|left|200px]]<br /><applet load="1pvz" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1pvz" />
 '''Solution Structure of BmP07, A Novel Potassium Channel Blocker from Scorpion Buthus martensi Karsch, 15 structures'''<br />
 ==Overview==
-A natural K+ channel blocker, BmKK2 (a member of scorpion toxin subfamily, alpha-KTx 14), which is composed of 31 amino acid residues and purified, from the venom of the Chinese scorpion Buthus martensi Karsch, was, characterized using whole-cell patch-clamp recording in rat hippocampal, neurons. The three dimensional structure of BmKK2 was determined with, two-dimensional NMR spectroscopy and molecular modelling techniques. In, solution this toxin adopted a common alpha/beta-motif, but showed distinct, local conformation in the loop between alpha-helix and beta-sheet in, comparison with typical short-chain scorpion toxins (e.g., CTX and NTX)., Also, the alpha helix is shorter and the beta-sheet element is smaller, (each strand consisted only two residues). The unusual structural feature, of BmKK2 was attributed to the shorter loop between the alpha-helix and, beta-sheet and the presence of two consecutive Pro residues at position 21, and 22 in the loop. Moreover, two models of BmKK2/hKv1.3 channel and, BmKK2/rSK2 channel complexes were simulated with docking calculations. The, results demonstrated the existence of a alpha-mode binding between the, toxin and the channels. The model of BmKK2/rSK2 channel complex exhibited, favorable contacts both in electrostatic and hydrophobic, including a, network of five hydrogen bonds and bigger interface containing seven pairs, of inter-residue interactions. In contrast, the model of BmKK2/hKv1.3, channel complex, containing only three pairs of inter-residue, interactions, exhibited poor contacts and smaller interface. The results, well explained its lower activity towards Kv channel, and predicted that, it may prefer a type of SK channel with a narrower entryway as its, specific receptor.
+A natural K+ channel blocker, BmKK2 (a member of scorpion toxin subfamily alpha-KTx 14), which is composed of 31 amino acid residues and purified from the venom of the Chinese scorpion Buthus martensi Karsch, was characterized using whole-cell patch-clamp recording in rat hippocampal neurons. The three dimensional structure of BmKK2 was determined with two-dimensional NMR spectroscopy and molecular modelling techniques. In solution this toxin adopted a common alpha/beta-motif, but showed distinct local conformation in the loop between alpha-helix and beta-sheet in comparison with typical short-chain scorpion toxins (e.g., CTX and NTX). Also, the alpha helix is shorter and the beta-sheet element is smaller (each strand consisted only two residues). The unusual structural feature of BmKK2 was attributed to the shorter loop between the alpha-helix and beta-sheet and the presence of two consecutive Pro residues at position 21 and 22 in the loop. Moreover, two models of BmKK2/hKv1.3 channel and BmKK2/rSK2 channel complexes were simulated with docking calculations. The results demonstrated the existence of a alpha-mode binding between the toxin and the channels. The model of BmKK2/rSK2 channel complex exhibited favorable contacts both in electrostatic and hydrophobic, including a network of five hydrogen bonds and bigger interface containing seven pairs of inter-residue interactions. In contrast, the model of BmKK2/hKv1.3 channel complex, containing only three pairs of inter-residue interactions, exhibited poor contacts and smaller interface. The results well explained its lower activity towards Kv channel, and predicted that it may prefer a type of SK channel with a narrower entryway as its specific receptor.
 ==About this Structure==
-PVZ 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=1PVZ OCA].
+PVZ 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=1PVZ OCA].
 ==Reference==
@@ Line 22: / Line 22: @@
 [[Category: alpha/beta scaffold]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:10:23 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:33:05 2008''