1pvz: Difference between revisions
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[[Image:1pvz.gif|left|200px]] | [[Image:1pvz.gif|left|200px]] | ||
'''Solution Structure of BmP07, A Novel Potassium Channel Blocker from Scorpion Buthus martensi Karsch, 15 structures''' | {{Structure | ||
|PDB= 1pvz |SIZE=350|CAPTION= <scene name='initialview01'>1pvz</scene> | |||
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'''Solution Structure of BmP07, A Novel Potassium Channel Blocker from Scorpion Buthus martensi Karsch, 15 structures''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1PVZ is a [ | 1PVZ is a [[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== | ==Reference== | ||
Solution structure of BmKK2, a new potassium channel blocker from the venom of chinese scorpion Buthus martensi Karsch., Zhang N, Li M, Chen X, Wang Y, Wu G, Hu G, Wu H, Proteins. 2004 Jun 1;55(4):835-45. PMID:[http:// | Solution structure of BmKK2, a new potassium channel blocker from the venom of chinese scorpion Buthus martensi Karsch., Zhang N, Li M, Chen X, Wang Y, Wu G, Hu G, Wu H, Proteins. 2004 Jun 1;55(4):835-45. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15146482 15146482] | ||
[[Category: Mesobuthus martensii]] | [[Category: Mesobuthus martensii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: alpha/beta scaffold]] | [[Category: alpha/beta scaffold]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:29:40 2008'' | ||
Revision as of 11:29, 20 March 2008
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Solution Structure of BmP07, A Novel Potassium Channel Blocker from Scorpion Buthus martensi Karsch, 15 structures
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.
About this Structure
1PVZ is a Single protein structure of sequence from Mesobuthus martensii. Full crystallographic information is available from OCA.
Reference
Solution structure of BmKK2, a new potassium channel blocker from the venom of chinese scorpion Buthus martensi Karsch., Zhang N, Li M, Chen X, Wang Y, Wu G, Hu G, Wu H, Proteins. 2004 Jun 1;55(4):835-45. PMID:15146482
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