3f1i

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (00:27, 28 December 2023) (edit) (undo)
 
(6 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:3f1i.png|left|200px]]
 
-
{{STRUCTURE_3f1i| PDB=3f1i | SCENE= }}
+
==Human ESCRT-0 Core Complex==
 +
<StructureSection load='3f1i' size='340' side='right'caption='[[3f1i]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[3f1i]] is a 3 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=3F1I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F1I 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]] 2.3&#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=3f1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f1i OCA], [https://pdbe.org/3f1i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f1i RCSB], [https://www.ebi.ac.uk/pdbsum/3f1i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f1i ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/HGS_HUMAN HGS_HUMAN] Involved in intracellular signal transduction mediated by cytokines and growth factors. When associated with STAM, it suppresses DNA signaling upon stimulation by IL-2 and GM-CSF. Could be a direct effector of PI3-kinase in vesicular pathway via early endosomes and may regulate trafficking to early and late endosomes by recruiting clathrin. May concentrate ubiquitinated receptors within clathrin-coated regions. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with STAM (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes. May contribute to the efficient recruitment of SMADs to the activin receptor complex. Involved in receptor recycling via its association with the CART complex, a multiprotein complex required for efficient transferrin receptor recycling but not for EGFR degradation.
 +
== 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/f1/3f1i_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=3f1i ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The human Hrs and STAM proteins comprise the ESCRT-0 complex, which sorts ubiquitinated cell surface receptors to lysosomes for degradation. Here we report a model for the complete ESCRT-0 complex based on the crystal structure of the Hrs-STAM core complex, previously solved domain structures, hydrodynamic measurements, and Monte Carlo simulations. ESCRT-0 expressed in insect cells has a hydrodynamic radius of RH = 7.9 nm and is a 1:1 heterodimer. The 2.3 Angstroms crystal structure of the ESCRT-0 core complex reveals two domain-swapped GAT domains and an antiparallel two-stranded coiled-coil, similar to yeast ESCRT-0. ESCRT-0 typifies a class of biomolecular assemblies that combine structured and unstructured elements, and have dynamic and open conformations to ensure versatility in target recognition. Coarse-grained Monte Carlo simulations constrained by experimental RH values for ESCRT-0 reveal a dynamic ensemble of conformations well suited for diverse functions.
-
===Human ESCRT-0 Core Complex===
+
Hybrid structural model of the complete human ESCRT-0 complex.,Ren X, Kloer DP, Kim YC, Ghirlando R, Saidi LF, Hummer G, Hurley JH Structure. 2009 Mar 11;17(3):406-16. PMID:19278655<ref>PMID:19278655</ref>
-
{{ABSTRACT_PUBMED_19278655}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
==About this Structure==
+
<div class="pdbe-citations 3f1i" style="background-color:#fffaf0;"></div>
-
[[3f1i]] is a 3 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=3F1I OCA].
+
== References ==
-
 
+
<references/>
-
==Reference==
+
__TOC__
-
<ref group="xtra">PMID:019278655</ref><references group="xtra"/>
+
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Ghirlando, R.]]
+
[[Category: Large Structures]]
-
[[Category: Hummer, G.]]
+
[[Category: Ghirlando R]]
-
[[Category: Hurley, J H.]]
+
[[Category: Hummer G]]
-
[[Category: Kim, Y.]]
+
[[Category: Hurley JH]]
-
[[Category: Kloer, D P.]]
+
[[Category: Kim Y]]
-
[[Category: Ren, X.]]
+
[[Category: Kloer DP]]
-
[[Category: Saidi, L.]]
+
[[Category: Ren X]]
-
[[Category: Endosome]]
+
[[Category: Saidi L]]
-
[[Category: Escrt]]
+
-
[[Category: Hg]]
+
-
[[Category: Membrane]]
+
-
[[Category: Metal-binding]]
+
-
[[Category: Mvb]]
+
-
[[Category: Phosphoprotein]]
+
-
[[Category: Protein binding]]
+
-
[[Category: Protein transport]]
+
-
[[Category: Sh3 domain]]
+
-
[[Category: Stam]]
+
-
[[Category: Transport]]
+
-
[[Category: Ubiquitin]]
+
-
[[Category: Zinc-finger]]
+

Current revision

Human ESCRT-0 Core Complex

PDB ID 3f1i

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/3f1i"
Personal tools