This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1hp2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1hp2.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1hp2.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1hp2| PDB=1hp2 | SCENE= }}
{{STRUCTURE_1hp2| PDB=1hp2 | SCENE= }}
-
'''SOLUTION STRUCTURE OF A TOXIN FROM THE SCORPION TITYUS SERRULATUS (TSTX-K ALPHA) DETERMINED BY NMR.'''
+
===SOLUTION STRUCTURE OF A TOXIN FROM THE SCORPION TITYUS SERRULATUS (TSTX-K ALPHA) DETERMINED BY NMR.===
-
==Overview==
+
<!--
-
A toxin from the scorpion Tityus serrulatus (TsTX-Kalpha) blocks native squid K(+) channels and their cloned counterpart, sqKv1A, at pH 8 ((native)K(d) approximately 20 nM; (sqKv1A)K(d) approximately 10 nM). In both cases, decreasing the pH below 7.0 significantly diminishes the TsTX-Kalpha effect (pK = 6.6). In the cloned squid channel, the pH dependence of the block is abolished by a single point mutation (H351G), and no change in toxin affinity was observed at higher pH values (pH &gt; or =8.0). To further investigate the TsTX-Kalpha-sqKv1A interaction, the three-dimensional structure of TsTX-Kalpha was determined in solution by NMR spectroscopy, and a model of the TsTX-Kalpha-sqKv1A complex was generated. As found for other alpha-K toxins such as charybdotoxin (CTX), site-directed mutagenesis at toxin residue K27 (K27A, K27R, and K27E) significantly reduced the toxin's affinity for sqKv1A channels. This is consistent with the TsTX-Kalpha-sqKv1A model reported here, which has K27 of the toxin inserted into the ion conduction pathway of the K(+) channel. This toxin-channel model also illustrates a possible mechanism for the pH-dependent block whereby lysine residues from TsTX-Kalpha (K6 and K23) are repelled by protonated H351 on sqKv1A at low pH.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11352729}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11352729 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11352729}}
==About this Structure==
==About this Structure==
-
1HP2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Tityus_serrulatus Tityus serrulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HP2 OCA].
+
1HP2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Tityus_serrulatus Tityus serrulatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HP2 OCA].
==Reference==
==Reference==
Line 30: Line 34:
[[Category: K+ channel]]
[[Category: K+ channel]]
[[Category: Scorpion toxin]]
[[Category: Scorpion toxin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:04:59 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:29:22 2008''

Revision as of 05:29, 1 July 2008

Image:1hp2.png

Template:STRUCTURE 1hp2

SOLUTION STRUCTURE OF A TOXIN FROM THE SCORPION TITYUS SERRULATUS (TSTX-K ALPHA) DETERMINED BY NMR.

Template:ABSTRACT PUBMED 11352729

About this Structure

1HP2 is a Single protein structure of sequence from Tityus serrulatus. Full experimental information is available from OCA.

Reference

Interaction of a toxin from the scorpion Tityus serrulatus with a cloned K+ channel from squid (sqKv1A)., Ellis KC, Tenenholz TC, Jerng H, Hayhurst M, Dudlak CS, Gilly WF, Blaustein MP, Weber DJ, Biochemistry. 2001 May 22;40(20):5942-53. PMID:11352729

Page seeded by OCA on Tue Jul 1 08:29:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hp2"
Personal tools