2zvo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "2zvo" [edit=sysop:move=sysop])
Current revision (19:19, 29 May 2024) (edit) (undo)
 
(8 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2zvo.png|left|200px]]
 
-
<!--
+
==NEMO CoZi domain in complex with diubiquitin in C2 space group==
-
The line below this paragraph, containing "STRUCTURE_2zvo", creates the "Structure Box" on the page.
+
<StructureSection load='2zvo' size='340' side='right'caption='[[2zvo]], [[Resolution|resolution]] 2.90&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'>[[2zvo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZVO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZVO 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]] 2.9&#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=2zvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zvo OCA], [https://pdbe.org/2zvo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zvo RCSB], [https://www.ebi.ac.uk/pdbsum/2zvo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zvo ProSAT]</span></td></tr>
-
{{STRUCTURE_2zvo| PDB=2zvo | SCENE= }}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/UBC_HUMAN UBC_HUMAN] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</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/zv/2zvo_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=2zvo ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Activation of nuclear factor-kappaB (NF-kappaB), a key mediator of inducible transcription in immunity, requires binding of NF-kappaB essential modulator (NEMO) to ubiquitinated substrates. Here, we report that the UBAN (ubiquitin binding in ABIN and NEMO) motif of NEMO selectively binds linear (head-to-tail) ubiquitin chains. Crystal structures of the UBAN motif revealed a parallel coiled-coil dimer that formed a heterotetrameric complex with two linear diubiquitin molecules. The UBAN dimer contacted all four ubiquitin moieties, and the integrity of each binding site was required for efficient NF-kappaB activation. Binding occurred via a surface on the proximal ubiquitin moiety and the canonical Ile44 surface on the distal one, thereby providing specificity for linear chain recognition. Residues of NEMO involved in binding linear ubiquitin chains are required for NF-kappaB activation by TNF-alpha and other agonists, providing an explanation for the detrimental effect of NEMO mutations in patients suffering from X-linked ectodermal dysplasia and immunodeficiency.
-
===NEMO CoZi domain in complex with diubiquitin in C2 space group===
+
Specific recognition of linear ubiquitin chains by NEMO is important for NF-kappaB activation.,Rahighi S, Ikeda F, Kawasaki M, Akutsu M, Suzuki N, Kato R, Kensche T, Uejima T, Bloor S, Komander D, Randow F, Wakatsuki S, Dikic I Cell. 2009 Mar 20;136(6):1098-109. PMID:19303852<ref>PMID:19303852</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_19303852}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 2zvo" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 19303852 is the PubMed ID number.
+
-
-->
+
-
{{ABSTRACT_PUBMED_19303852}}
+
-
 
+
-
==About this Structure==
+
-
[[2zvo]] is a 4 chain structure of [[Ubiquitin]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZVO OCA].
+
==See Also==
==See Also==
-
*[[Ubiquitin]]
+
*[[3D structures of ubiquitin|3D structures of ubiquitin]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:19303852</ref><references group="xtra"/>
+
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
 +
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
-
[[Category: Akutsu, M.]]
+
[[Category: Akutsu M]]
-
[[Category: Bloor, S.]]
+
[[Category: Bloor S]]
-
[[Category: Dikic, I.]]
+
[[Category: Dikic I]]
-
[[Category: Ikeda, F.]]
+
[[Category: Ikeda F]]
-
[[Category: Kato, R.]]
+
[[Category: Kato R]]
-
[[Category: Kawasaki, M.]]
+
[[Category: Kawasaki M]]
-
[[Category: Kensche, T.]]
+
[[Category: Kensche T]]
-
[[Category: Komander, D.]]
+
[[Category: Komander D]]
-
[[Category: Rahighi, S.]]
+
[[Category: Rahighi S]]
-
[[Category: Randow, F.]]
+
[[Category: Randow F]]
-
[[Category: Suzuki, N.]]
+
[[Category: Suzuki N]]
-
[[Category: Uejima, T.]]
+
[[Category: Uejima T]]
-
[[Category: Wakatsuki, S.]]
+
[[Category: Wakatsuki S]]
-
[[Category: Coiled coil]]
+
-
[[Category: Cytoplasm]]
+
-
[[Category: Metal-binding]]
+
-
[[Category: Nf-kb signaling]]
+
-
[[Category: Nucleus]]
+
-
[[Category: Phosphoprotein]]
+
-
[[Category: Transcription]]
+
-
[[Category: Transcription regulation]]
+
-
[[Category: Transcription/signaling protein complex]]
+
-
[[Category: Ubiquitin binding]]
+
-
[[Category: Ubl conjugation]]
+
-
[[Category: Zinc]]
+
-
[[Category: Zinc-finger]]
+

Current revision

NEMO CoZi domain in complex with diubiquitin in C2 space group

PDB ID 2zvo

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/2zvo"
Personal tools