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.


1koz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1koz.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1koz.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1koz| PDB=1koz | SCENE= }}
{{STRUCTURE_1koz| PDB=1koz | SCENE= }}
-
'''SOLUTION STRUCTURE OF OMEGA-GRAMMOTOXIN SIA'''
+
===SOLUTION STRUCTURE OF OMEGA-GRAMMOTOXIN SIA===
-
==Overview==
+
<!--
-
omega-Grammotoxin SIA (GrTx) is a 36 amino acid residue protein toxin from spider venom that inhibits P/Q and N-type voltage-gated Ca(2+) channels by modifying voltage-dependent gating. We determined the three-dimensional structure of GrTx using NMR spectroscopy. The toxin adopts an "inhibitor cystine knot" motif composed of two beta-strands (Leu19-Cys21 and Cys30-Trp32) and a beta-bulge (Trp6, Gly7-Cys30) with a +2x, -1 topology, which are connected by four chain reversals. Although GrTx was originally identified as an inhibitor of voltage-gated Ca(2+) channel, it also binds to K(+) channels with lower affinity. A similar cross-reaction was observed for Hanatoxin1 (HaTx), which binds to the voltage-sensing domains of K(+) and Ca(2+) channels with different affinities. A detailed comparison of the GrTx and HaTx structures identifies a conserved face containing a large hydrophobic patch surrounded by positively charged residues. The slight differences in the surface shape, which result from the orientation of the surface aromatic residues and/or the distribution of the charged residues, may explain the differences in the binding affinity of these gating modifiers with different voltage-gated ion channels.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12162963}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12162963 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12162963}}
==About this Structure==
==About this Structure==
-
1KOZ is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KOZ OCA].
+
1KOZ is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KOZ OCA].
==Reference==
==Reference==
Line 30: Line 34:
[[Category: Cystine knot]]
[[Category: Cystine knot]]
[[Category: Toxin]]
[[Category: Toxin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:59:58 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:40:59 2008''

Revision as of 07:41, 2 July 2008

Image:1koz.png

Template:STRUCTURE 1koz

SOLUTION STRUCTURE OF OMEGA-GRAMMOTOXIN SIA

Template:ABSTRACT PUBMED 12162963

About this Structure

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

Reference

Solution structure of omega-grammotoxin SIA, a gating modifier of P/Q and N-type Ca(2+) channel., Takeuchi K, Park E, Lee C, Kim J, Takahashi H, Swartz K, Shimada I, J Mol Biol. 2002 Aug 16;321(3):517-26. PMID:12162963

Page seeded by OCA on Wed Jul 2 10:40:59 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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