3m0d

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "3m0d" [edit=sysop:move=sysop])
Current revision (08:46, 6 September 2023) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
-
{{STRUCTURE_3m0d| PDB=3m0d | SCENE= }}
 
-
===Crystal structure of the TRAF1:TRAF2:cIAP2 complex===
 
-
{{ABSTRACT_PUBMED_20385093}}
 
-
==Disease==
+
==Crystal structure of the TRAF1:TRAF2:cIAP2 complex==
-
[[http://www.uniprot.org/uniprot/BIRC3_HUMAN BIRC3_HUMAN]] Note=A chromosomal aberration involving BIRC3 is recurrent in low-grade mucosa-associated lymphoid tissue (MALT lymphoma). Translocation t(11;18)(q21;q21) with MALT1. This translocation is found in approximately 50% of cytogenetically abnormal low-grade MALT lymphoma.
+
<StructureSection load='3m0d' size='340' side='right'caption='[[3m0d]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[3m0d]] is a 4 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=3M0D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M0D 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]] 2.8&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=3m0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m0d OCA], [https://pdbe.org/3m0d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m0d RCSB], [https://www.ebi.ac.uk/pdbsum/3m0d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m0d ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/TRAF2_HUMAN TRAF2_HUMAN] Regulates activation of NF-kappa-B and JNK and plays a central role in the regulation of cell survival and apoptosis. Required for normal antibody isotype switching from IgM to IgG. Has E3 ubiquitin-protein ligase activity and promotes 'Lys-63'-linked ubiquitination of target proteins, such as BIRC3, RIPK1 and TICAM1. Is an essential constituent of several E3 ubiquitin-protein ligase complexes, where it promotes the ubiquitination of target proteins by bringing them into contact with other E3 ubiquitin ligases. Regulates BIRC2 and BIRC3 protein levels by inhibiting their autoubiquitination and subsequent degradation; this does not depend on the TRAF2 RING-type zinc finger domain.<ref>PMID:10346818</ref> <ref>PMID:11907583</ref> <ref>PMID:12917689</ref> <ref>PMID:15383523</ref> <ref>PMID:19506082</ref> <ref>PMID:19150425</ref> <ref>PMID:18981220</ref> <ref>PMID:19918265</ref> <ref>PMID:20064526</ref> <ref>PMID:19937093</ref> <ref>PMID:20047764</ref> <ref>PMID:20577214</ref> <ref>PMID:19810754</ref> <ref>PMID:20385093</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/m0/3m0d_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=3m0d ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
TRAF1/2 and cIAP1/2 are members of the TNF receptor-associated factor (TRAF) and the inhibitor of apoptosis (IAP) families, respectively. They are critical for canonical and noncanonical NF-kappaB signaling pathways. Here, we report the crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 complexes. A TRAF2 trimer interacts with one cIAP2 both in the crystal and in solution. Two chains of the TRAF2 trimer directly contact cIAP2, and key residues at the interface are confirmed by mutagenesis. TRAF1 and TRAF2 preferentially form the TRAF1: (TRAF2)(2) heterotrimer, which interacts with cIAP2 more strongly than TRAF2 alone. In contrast, TRAF1 alone interacts very weakly with cIAP2. Surprisingly, TRAF1 and one chain of TRAF2 in the TRAF1: (TRAF2)(2): cIAP2 ternary complex mediate interaction with cIAP2. Because TRAF1 is upregulated by many stimuli, it may modulate the interaction of TRAF2 with cIAP1/2, which explains regulatory roles of TRAF1 in TNF signaling.
-
==Function==
+
Crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 complexes: affinity, specificity, and regulation.,Zheng C, Kabaleeswaran V, Wang Y, Cheng G, Wu H Mol Cell. 2010 Apr 9;38(1):101-13. PMID:20385093<ref>PMID:20385093</ref>
-
[[http://www.uniprot.org/uniprot/TRAF2_HUMAN TRAF2_HUMAN]] Regulates activation of NF-kappa-B and JNK and plays a central role in the regulation of cell survival and apoptosis. Required for normal antibody isotype switching from IgM to IgG. Has E3 ubiquitin-protein ligase activity and promotes 'Lys-63'-linked ubiquitination of target proteins, such as BIRC3, RIPK1 and TICAM1. Is an essential constituent of several E3 ubiquitin-protein ligase complexes, where it promotes the ubiquitination of target proteins by bringing them into contact with other E3 ubiquitin ligases. Regulates BIRC2 and BIRC3 protein levels by inhibiting their autoubiquitination and subsequent degradation; this does not depend on the TRAF2 RING-type zinc finger domain.<ref>PMID:10346818</ref><ref>PMID:11907583</ref><ref>PMID:12917689</ref><ref>PMID:15383523</ref><ref>PMID:19506082</ref><ref>PMID:19150425</ref><ref>PMID:18981220</ref><ref>PMID:19918265</ref><ref>PMID:20064526</ref><ref>PMID:19937093</ref><ref>PMID:20047764</ref><ref>PMID:20577214</ref><ref>PMID:19810754</ref><ref>PMID:20385093</ref> [[http://www.uniprot.org/uniprot/BIRC3_HUMAN BIRC3_HUMAN]] Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, TRAF1, and BCL10. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8.<ref>PMID:21931591</ref> [[http://www.uniprot.org/uniprot/TRAF1_HUMAN TRAF1_HUMAN]] Adapter molecule that regulates the activation of NF-kappa-B and JNK. Plays a role in the regulation of cell survival and apoptosis. The heterotrimer formed by TRAF1 and TRAF2 is part of a E3 ubiquitin-protein ligase complex that promotes ubiquitination of target proteins, such as MAP3K14. The TRAF1/TRAF2 complex recruits the antiapoptotic E3 protein-ubiquitin ligases BIRC2 and BIRC3 to TNFRSF1B/TNFR2.<ref>PMID:10692572</ref><ref>PMID:16323247</ref><ref>PMID:18429822</ref><ref>PMID:19698991</ref><ref>PMID:19287455</ref><ref>PMID:20385093</ref>
+
-
==About this Structure==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[3m0d]] is a 4 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=3M0D OCA].
+
</div>
 +
<div class="pdbe-citations 3m0d" style="background-color:#fffaf0;"></div>
-
==Reference==
+
==See Also==
-
<ref group="xtra">PMID:020385093</ref><references group="xtra"/><references/>
+
*[[TNF receptor-associated factor 3D structures|TNF receptor-associated factor 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Kabaleeswaran, V.]]
+
[[Category: Large Structures]]
-
[[Category: Wu, H.]]
+
[[Category: Kabaleeswaran V]]
-
[[Category: Apoptosis]]
+
[[Category: Wu H]]
-
[[Category: Metal-binding]]
+
-
[[Category: Signaling protein]]
+
-
[[Category: Trimeric helix coiled coiled]]
+

Current revision

Crystal structure of the TRAF1:TRAF2:cIAP2 complex

PDB ID 3m0d

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/3m0d"
Personal tools