1hp9: Difference between revisions

Revision as of 08:29, 1 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:1hp9.png

Template:STRUCTURE 1hp9

kappa-Hefutoxins: a novel Class of Potassium Channel Toxins from Scorpion venomkappa-Hefutoxins: a novel Class of Potassium Channel Toxins from Scorpion venom

Template:ABSTRACT PUBMED 12034709

About this StructureAbout this Structure

1HP9 is a Single protein structure. Full experimental information is available from OCA.

ReferenceReference

kappa-Hefutoxin1, a novel toxin from the scorpion Heterometrus fulvipes with unique structure and function. Importance of the functional diad in potassium channel selectivity., Srinivasan KN, Sivaraja V, Huys I, Sasaki T, Cheng B, Kumar TK, Sato K, Tytgat J, Yu C, San BC, Ranganathan S, Bowie HJ, Kini RM, Gopalakrishnakone P, J Biol Chem. 2002 Aug 16;277(33):30040-7. Epub 2002 May 28. PMID:12034709

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OCA

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-'''kappa-Hefutoxins: a novel Class of Potassium Channel Toxins from Scorpion venom'''
+===kappa-Hefutoxins: a novel Class of Potassium Channel Toxins from Scorpion venom===
-==Overview==
+<!--
-An important and exciting challenge in the postgenomic era is to understand the functions of newly discovered proteins based on their structures. The main thrust is to find the common structural motifs that contribute to specific functions. Using this premise, here we report the purification, solution NMR, and functional characterization of a novel class of weak potassium channel toxins from the venom of the scorpion Heterometrus fulvipes. These toxins, kappa-hefutoxin1 and kappa-hefutoxin2, exhibit no homology to any known toxins. NMR studies indicate that kappa-hefutoxin1 adopts a unique three-dimensional fold of two parallel helices linked by two disulfide bridges without any beta-sheets. Based on the presence of the functional diad (Tyr(5)/Lys(19)) at a distance (6.0 +/- 1.0 A) comparable with other potassium channel toxins, we hypothesized its function as a potassium channel toxin. kappa-Hefutoxin 1 not only blocks the voltage-gated K(+)-channels, Kv1.3 and Kv1.2, but also slows the activation kinetics of Kv1.3 currents, a novel feature of kappa-hefutoxin 1, unlike other scorpion toxins, which are considered solely pore blockers. Alanine mutants (Y5A, K19A, and Y5A/K19A) failed to block the channels, indicating the importance of the functional diad.
+The line below this paragraph, {{ABSTRACT_PUBMED_12034709}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12034709 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12034709}}
 ==About this Structure==
-HP9 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HP9 OCA].
+HP9 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HP9 OCA].
 ==Reference==
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 [[Category: Scorpion toxin]]
 [[Category: Voltage-gated potassium channel]]
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