3ddt: Difference between revisions

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New page: '''Unreleased structure''' The entry 3ddt is ON HOLD until Paper Publication Authors: Mrosek, M., Meier, S., Ucurum-Fotiadis, Z., von Castelmur, E., Hedbom, E., Lustig, A., Grzesiek, S....
 
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'''Unreleased structure'''


The entry 3ddt is ON HOLD  until Paper Publication
==Crystal structure of the B2 box from MuRF1 in dimeric state==
<StructureSection load='3ddt' size='340' side='right'caption='[[3ddt]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ddt]] 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=3DDT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DDT 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]] 1.9&#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=3ddt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ddt OCA], [https://pdbe.org/3ddt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ddt RCSB], [https://www.ebi.ac.uk/pdbsum/3ddt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ddt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TRI63_HUMAN TRI63_HUMAN] E3 ubiquitin ligase. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells.<ref>PMID:11927605</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/dd/3ddt_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=3ddt ConSurf].
<div style="clear:both"></div>


Authors: Mrosek, M., Meier, S., Ucurum-Fotiadis, Z., von Castelmur, E., Hedbom, E., Lustig, A., Grzesiek, S., Labeit, D., Labeit, S., Mayans, O.
==See Also==
 
*[[Mur ligase|Mur ligase]]
Description: Crystal structure of the B2 box from MuRF1 in dimeric state
*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
 
== References ==
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Jul 11 13:06:40 2008''
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Mayans O]]
[[Category: Mrosek M]]

Latest revision as of 11:23, 20 March 2024

Crystal structure of the B2 box from MuRF1 in dimeric stateCrystal structure of the B2 box from MuRF1 in dimeric state

Structural highlights

3ddt is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TRI63_HUMAN E3 ubiquitin ligase. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. McElhinny AS, Kakinuma K, Sorimachi H, Labeit S, Gregorio CC. Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1. J Cell Biol. 2002 Apr 1;157(1):125-36. Epub 2002 Apr 1. PMID:11927605 doi:http://dx.doi.org/10.1083/jcb.200108089

3ddt, resolution 1.90Å

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