1q2k: Difference between revisions

Revision as of 12:05, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1q2k.png

Template:STRUCTURE 1q2k

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

Template:ABSTRACT PUBMED 15049683

About this StructureAbout this Structure

1Q2K is a Single protein structure. Full experimental information is available from OCA.

ReferenceReference

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

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_1q2k|  PDB=1q2k  |  SCENE=  }}
-'''Solution structure of BmBKTx1 a new potassium channel blocker from the Chinese Scorpion Buthus martensi Karsch'''
+===Solution structure of BmBKTx1 a new potassium channel blocker from the Chinese Scorpion Buthus martensi Karsch===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15049683}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15049683 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15049683}}
 ==About this Structure==
-Q2K is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q2K OCA].
+Q2K is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q2K OCA].
 ==Reference==
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 [[Category: Alpha-helix]]
 [[Category: Beta-sheet]]
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