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.


2wvn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:17, 9 May 2024) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:2wvn.jpg|left|200px]]
 
-
<!--
+
==Structure of the HET-s N-terminal domain==
-
The line below this paragraph, containing "STRUCTURE_2wvn", creates the "Structure Box" on the page.
+
<StructureSection load='2wvn' size='340' side='right'caption='[[2wvn]], [[Resolution|resolution]] 2.62&Aring;' 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'>[[2wvn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Podospora_anserina Podospora anserina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WVN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WVN 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">X-ray diffraction, [[Resolution|Resolution]] 2.62&#8491;</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=2wvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wvn OCA], [https://pdbe.org/2wvn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wvn RCSB], [https://www.ebi.ac.uk/pdbsum/2wvn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wvn ProSAT]</span></td></tr>
-
{{STRUCTURE_2wvn| PDB=2wvn | SCENE= }}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/HETS_PODAS HETS_PODAS] Responsible for heterokaryon incompatibility, a process that ensures that during spontaneous, vegetative cell fusion only compatible cells from the same colony survive (non-self-recognition). Forms a prion for the non-Mendelian trait [het-s]. Interacts with het-S from incompatible cells to trigger a lethal reaction that prevents the formation of viable heterokaryons. It is unknown if the native, soluble protein has a cellular function.<ref>PMID:1886611</ref> <ref>PMID:8224826</ref> <ref>PMID:9275200</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wv/2wvn_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2wvn ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
HET-S (97% identical to HET-s) has an N-terminal globular domain that exerts a prion-inhibitory effect in cis on its own prion-forming domain (PFD) and in trans on HET-s prion propagation. We show that HET-S fails to form fibrils in vitro and that it inhibits HET-s PFD fibrillization in trans. In vivo analyses indicate that beta-structuring of the HET-S PFD is required for HET-S activity. The crystal structures of the globular domains of HET-s and HET-S are highly similar, comprising a helical fold, while NMR-based characterizations revealed no differences in the conformations of the PFDs. We conclude that prion inhibition is not encoded by structure but rather in stability and oligomerization properties: when HET-S forms a prion seed or is incorporated into a HET-s fibril via its PFD, the beta-structuring in this domain induces a change in its globular domain, generating a molecular species that is incompetent for fibril growth.
-
===STRUCTURE OF THE HET-S N-TERMINAL DOMAIN===
+
The mechanism of prion inhibition by HET-S.,Greenwald J, Buhtz C, Ritter C, Kwiatkowski W, Choe S, Maddelein ML, Ness F, Cescau S, Soragni A, Leitz D, Saupe SJ, Riek R Mol Cell. 2010 Jun 25;38(6):889-99. PMID:20620958<ref>PMID:20620958</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2wvn" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_20620958}}, adds the Publication Abstract to the page
+
*[[Prion 3D structures|Prion 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 20620958 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_20620958}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Large Structures]]
-
2WVN is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Podospora_anserina Podospora anserina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WVN OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:20620958</ref><references group="xtra"/>
+
[[Category: Podospora anserina]]
[[Category: Podospora anserina]]
-
[[Category: Buhtz, C.]]
+
[[Category: Buhtz C]]
-
[[Category: Choe, S.]]
+
[[Category: Choe S]]
-
[[Category: Greenwald, J.]]
+
[[Category: Greenwald J]]
-
[[Category: Kwiatkowski, W.]]
+
[[Category: Kwiatkowski W]]
-
[[Category: Riek, R.]]
+
[[Category: Riek R]]
-
[[Category: Ritter, C.]]
+
[[Category: Ritter C]]
-
[[Category: Saupe, S J.]]
+
[[Category: Saupe SJ]]
-
[[Category: Heterokaryon incompatibility]]
+
-
[[Category: Prion regulatory domain]]
+
-
[[Category: Prion-binding protein]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 28 12:33:44 2010''
+

Current revision

Structure of the HET-s N-terminal domain

PDB ID 2wvn

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/2wvn"
Personal tools