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.


3frr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "3frr" [edit=sysop:move=sysop])
Current revision (06:50, 6 September 2023) (edit) (undo)
 
(4 intermediate revisions not shown.)
Line 1: Line 1:
-
{{STRUCTURE_3frr| PDB=3frr | SCENE= }}
 
-
===Structure of human IST1(NTD) - (residues 1-189)(P21)===
 
-
{{ABSTRACT_PUBMED_19525971}}
 
-
==About this Structure==
+
==Structure of human IST1(NTD) - (residues 1-189)(P21)==
-
[[3frr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FRR OCA].
+
<StructureSection load='3frr' size='340' side='right'caption='[[3frr]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[3frr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FRR FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#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=3frr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3frr OCA], [https://pdbe.org/3frr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3frr RCSB], [https://www.ebi.ac.uk/pdbsum/3frr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3frr ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/IST1_HUMAN IST1_HUMAN] Proposed to be involved in specific functions of the ESCRT machinery. Is required for efficient abscission during cytokinesis, but not for HIV-1 budding. The involvement in the MVB pathway is not established. Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells.<ref>PMID:19129479</ref> <ref>PMID:19129480</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/fr/3frr_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=3frr ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Endosomal sorting complexes required for transport-III (ESCRT-III) subunits cycle between two states: soluble monomers and higher-order assemblies that bind and remodel membranes during endosomal vesicle formation, midbody abscission and enveloped virus budding. Here we show that the N-terminal core domains of increased sodium tolerance-1 (IST1) and charged multivesicular body protein-3 (CHMP3) form equivalent four-helix bundles, revealing that IST1 is a previously unrecognized ESCRT-III family member. IST1 and its ESCRT-III binding partner, CHMP1B, both form higher-order helical structures in vitro, and IST1-CHMP1 interactions are required for abscission. The IST1 and CHMP3 structures also reveal that equivalent downstream alpha5 helices can fold back against the core domains. Mutations within the CHMP3 core-alpha5 interface stimulate the protein's in vitro assembly and HIV-inhibition activities, indicating that dissociation of the autoinhibitory alpha5 helix from the core activates ESCRT-III proteins for assembly at membranes.
-
==Reference==
+
Structural basis for ESCRT-III protein autoinhibition.,Bajorek M, Schubert HL, McCullough J, Langelier C, Eckert DM, Stubblefield WM, Uter NT, Myszka DG, Hill CP, Sundquist WI Nat Struct Mol Biol. 2009 Jul;16(7):754-62. Epub 2009 Jun 14. PMID:19525971<ref>PMID:19525971</ref>
-
<ref group="xtra">PMID:019525971</ref><references group="xtra"/><references/>
+
 
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 3frr" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Bajorek, M.]]
+
[[Category: Large Structures]]
-
[[Category: Hill, C P.]]
+
[[Category: Bajorek M]]
-
[[Category: Schubert, H L.]]
+
[[Category: Hill CP]]
-
[[Category: Sundquist, W I.]]
+
[[Category: Schubert HL]]
-
[[Category: Chmp]]
+
[[Category: Sundquist WI]]
-
[[Category: Escrt]]
+
-
[[Category: Escrt-iii]]
+
-
[[Category: Ist1]]
+
-
[[Category: Phosphoprotein]]
+
-
[[Category: Protein binding]]
+

Current revision

Structure of human IST1(NTD) - (residues 1-189)(P21)

PDB ID 3frr

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools