1q2k: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /><applet load="1q2k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q2k" /> '''Solution structure of BmBKTx1 a new potassiu...
 
OCA (talk | contribs)
No edit summary
 
(14 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1q2k.jpg|left|200px]]<br /><applet load="1q2k" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1q2k" />
'''Solution structure of BmBKTx1 a new potassium channel blocker from the Chinese Scorpion Buthus martensi Karsch'''<br />


==Overview==
==Solution structure of BmBKTx1 a new potassium channel blocker from the Chinese Scorpion Buthus martensi Karsch==
BmBKTx1 is a 31-amino acid peptide identified from the venom of the, Chinese scorpion Buthus martensi Karsch, blocking high-conductance, calcium-activated potassium channels. Sequence homology analysis indicates, that BmBKTx1 is a new subfamily of short-chain alpha-KTx toxins of the, potassium channel, which we term alpha-KTx19. Synthetic BmBKTx1 was, prepared by using solid-phase peptide synthesis. Two-dimensional NMR, spectroscopy techniques were used to determine the solution structure of, BmBKTx1. The results show that the BmBKTx1 forms a typical, cysteine-stabilized alpha/beta scaffold adopted by most short-chain, scorpion toxins. The structure of BmBKTx1 consists of a two-stranded, antiparallel beta-sheet (residues 20-29) and an alpha-helix (residues, 5-15). The three-dimensional structure of BmBKTx1 was also compared with, those of two function-related scorpion toxins, charybdotoxin (ChTx) and, BmTx1, and their structural and functional implications are discussed.
<StructureSection load='1q2k' size='340' side='right'caption='[[1q2k]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1q2k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mesobuthus_martensii Mesobuthus martensii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q2K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q2K FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 21 models</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1q2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q2k OCA], [https://pdbe.org/1q2k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q2k RCSB], [https://www.ebi.ac.uk/pdbsum/1q2k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q2k ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KA191_MESMA KA191_MESMA] Selective inhibitor of high conductance calcium-activated potassium channels KCa1.1/KCNMA1. May be insect specific.<ref>PMID:15178692</ref> [PDB:3E8Y]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BmBKTx1 is a 31-amino acid peptide identified from the venom of the Chinese scorpion Buthus martensi Karsch, blocking high-conductance calcium-activated potassium channels. Sequence homology analysis indicates that BmBKTx1 is a new subfamily of short-chain alpha-KTx toxins of the potassium channel, which we term alpha-KTx19. Synthetic BmBKTx1 was prepared by using solid-phase peptide synthesis. Two-dimensional NMR spectroscopy techniques were used to determine the solution structure of BmBKTx1. The results show that the BmBKTx1 forms a typical cysteine-stabilized alpha/beta scaffold adopted by most short-chain scorpion toxins. The structure of BmBKTx1 consists of a two-stranded antiparallel beta-sheet (residues 20-29) and an alpha-helix (residues 5-15). The three-dimensional structure of BmBKTx1 was also compared with those of two function-related scorpion toxins, charybdotoxin (ChTx) and BmTx1, and their structural and functional implications are discussed.


==About this Structure==
Solution structure of BmBKTx1, a new BKCa1 channel blocker from the Chinese scorpion Buthus martensi Karsch.,Cai Z, Xu C, Xu Y, Lu W, Chi CW, Shi Y, Wu J Biochemistry. 2004 Apr 6;43(13):3764-71. PMID:15049683<ref>PMID:15049683</ref>
1Q2K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q2K OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Solution structure of BmBKTx1, a new BKCa1 channel blocker from the Chinese scorpion Buthus martensi Karsch., Cai Z, Xu C, Xu Y, Lu W, Chi CW, Shi Y, Wu J, Biochemistry. 2004 Apr 6;43(13):3764-71. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15049683 15049683]
</div>
[[Category: Single protein]]
<div class="pdbe-citations 1q2k" style="background-color:#fffaf0;"></div>
[[Category: Cai, Z.]]
[[Category: Chi, C.W.]]
[[Category: Lu, W.]]
[[Category: Shi, Y.]]
[[Category: Wu, J.]]
[[Category: Xu, C.]]
[[Category: Xu, Y.]]
[[Category: alpha-helix]]
[[Category: beta-sheet]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:19:58 2007''
==See Also==
*[[Potassium channel toxin 3D structures|Potassium channel toxin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mesobuthus martensii]]
[[Category: Cai Z]]
[[Category: Chi CW]]
[[Category: Lu W]]
[[Category: Shi Y]]
[[Category: Wu J]]
[[Category: Xu C]]
[[Category: Xu Y]]

Latest revision as of 07:24, 9 October 2024

Solution structure of BmBKTx1 a new potassium channel blocker from the Chinese Scorpion Buthus martensi Karsch

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA