1y2p

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:43, 23 October 2024) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1y2p.png|left|200px]]
 
-
<!--
+
==Solution structure of Hstx3P==
-
The line below this paragraph, containing "STRUCTURE_1y2p", creates the "Structure Box" on the page.
+
<StructureSection load='1y2p' size='340' side='right'caption='[[1y2p]]' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1y2p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Heterometrus_spinifer Heterometrus spinifer]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y2P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y2P FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 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=1y2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y2p OCA], [https://pdbe.org/1y2p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y2p RCSB], [https://www.ebi.ac.uk/pdbsum/1y2p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y2p ProSAT]</span></td></tr>
-
{{STRUCTURE_1y2p| PDB=1y2p | SCENE= }}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/KAX63_HETSP KAX63_HETSP] Potently blocks voltage-gated potassium channels Kv1.1/KCNA1 and Kv1.3/KCNA3. Mildly blocks intermediate (IK) conductance calcium-activated potassium channels (KCa3.1/KCNN4) and ERG1/Kv11.1/KCNH2.<ref>PMID:15498765</ref> <ref>PMID:18687312</ref> <ref>PMID:9359871</ref>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Animal toxins are highly reticulated and structured polypeptides that adopt a limited number of folds. In scorpion species, the most represented fold is the alpha/beta scaffold in which an helical structure is connected to an antiparallel beta-sheet by two disulfide bridges. The intimate relationship existing between peptide reticulation and folding remains poorly understood. Here, we investigated the role of disulfide bridging on the 3D structure of HsTx1, a scorpion toxin potently active on Kv1.1 and Kv1.3 channels. This toxin folds along the classical alpha/beta scaffold but belongs to a unique family of short-chain, four disulfide-bridged toxins. Removal of the fourth disulfide bridge of HsTx1 does not affect its helical structure, whereas its two-stranded beta-sheet is altered from a twisted to a nontwisted configuration. This structural change in HsTx1 is accompanied by a marked decrease in Kv1.1 and Kv1.3 current blockage, and by alterations in the toxin to channel molecular contacts. In contrast, a similar removal of the fourth disulfide bridge of Pi1, another scorpion toxin from the same structural family, has no impact on its 3D structure, pharmacology, or channel interaction. These data highlight the importance of disulfide bridging in reaching the correct bioactive conformation of some toxins.
-
===Solution structure of Hstx3P===
+
The impact of the fourth disulfide bridge in scorpion toxins of the alpha-KTx6 subfamily.,Carrega L, Mosbah A, Ferrat G, Beeton C, Andreotti N, Mansuelle P, Darbon H, De Waard M, Sabatier JM Proteins. 2005 Dec 1;61(4):1010-23. PMID:16247791<ref>PMID:16247791</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1y2p" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_16247791}}, adds the Publication Abstract to the page
+
*[[Potassium channel toxin 3D structures|Potassium channel toxin 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 16247791 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_16247791}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Heterometrus spinifer]]
-
1Y2P is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y2P OCA].
+
[[Category: Large Structures]]
-
 
+
[[Category: Darbon H]]
-
==Reference==
+
[[Category: Gariga L]]
-
The impact of the fourth disulfide bridge in scorpion toxins of the alpha-KTx6 subfamily., Carrega L, Mosbah A, Ferrat G, Beeton C, Andreotti N, Mansuelle P, Darbon H, De Waard M, Sabatier JM, Proteins. 2005 Dec 1;61(4):1010-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16247791 16247791]
+
[[Category: Mosbah A]]
-
[[Category: Single protein]]
+
[[Category: Sabatier JM]]
-
[[Category: Darbon, H.]]
+
-
[[Category: Gariga, L.]]
+
-
[[Category: Mosbah, A.]]
+
-
[[Category: Sabatier, J M.]]
+
-
[[Category: Hstx3p]]
+
-
[[Category: Nmr structure]]
+
-
[[Category: Potassium channel]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 18:14:37 2008''
+

Current revision

Solution structure of Hstx3P

PDB ID 1y2p

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1y2p"
Personal tools