2fzp: Difference between revisions

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[[Image:2fzp.png|left|200px]]


{{STRUCTURE_2fzp|  PDB=2fzp  |  SCENE=  }}
==Crystal structure of the USP8 interaction domain of human NRDP1==
 
<StructureSection load='2fzp' size='340' side='right'caption='[[2fzp]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
===Crystal structure of the USP8 interaction domain of human NRDP1===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[2fzp]] 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=2FZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FZP FirstGlance]. <br>
{{ABSTRACT_PUBMED_17035239}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.87&#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=2fzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fzp OCA], [https://pdbe.org/2fzp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fzp RCSB], [https://www.ebi.ac.uk/pdbsum/2fzp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fzp ProSAT]</span></td></tr>
==About this Structure==
</table>
[[2fzp]] 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=2FZP OCA].  
== Function ==
 
[https://www.uniprot.org/uniprot/RNF41_HUMAN RNF41_HUMAN] Acts as E3 ubiquitin-protein ligase and regulates the degradation of target proteins. Polyubiquitinates MYD88 and Negatively regulates MYD88-dependent production of proinflammatory cytokines but can promote TRIF-dependent production of type I interferon. Promotes also activation of TBK1 and IRF3. Involved in the ubiquitination of erythropoietin (EPO) and interleukin-3 (IL-3) receptors. Thus, through maintaining basal levels of cytokine receptors, RNF41 is involved in the control of hematopoietic progenitor cell differentiation into myeloerythroid lineages (By similarity). Contributes to the maintenance of steady-state ERBB3 levels by mediating its growth factor-independent degradation. Involved in the degradation of the inhibitor of apoptosis BIRC6 and thus is an important regulator of cell death by promoting apoptosis. Acts also as a PARK2 modifier that accelerates its degradation, resulting in a reduction of PARK2 activity, influencing the balance of intracellular redox state.<ref>PMID:12411582</ref> <ref>PMID:14765125</ref> <ref>PMID:15632191</ref> <ref>PMID:17210635</ref> <ref>PMID:18541373</ref> <ref>PMID:19483718</ref>
==Reference==
== Evolutionary Conservation ==
<ref group="xtra">PMID:017035239</ref><ref group="xtra">PMID:015314180</ref><ref group="xtra">PMID:014765125</ref><ref group="xtra">PMID:011867753</ref><ref group="xtra">PMID:011358394</ref><references group="xtra"/>
[[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/fz/2fzp_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=2fzp ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Arrowsmith, C.]]
[[Category: Large Structures]]
[[Category: Avvakumov, G V.]]
[[Category: Arrowsmith C]]
[[Category: Bochkarev, A.]]
[[Category: Avvakumov GV]]
[[Category: Butler-Cole, C.]]
[[Category: Bochkarev A]]
[[Category: Dhe-Paganon, S.]]
[[Category: Butler-Cole C]]
[[Category: Edwards, A.]]
[[Category: Dhe-Paganon S]]
[[Category: Finerty, P J.]]
[[Category: Edwards A]]
[[Category: Newman, E M.]]
[[Category: Finerty Jr PJ]]
[[Category: SGC, Structural Genomics Consortium.]]
[[Category: Newman EM]]
[[Category: Sundstrom, M.]]
[[Category: Sundstrom M]]
[[Category: Walker, J R.]]
[[Category: Walker JR]]
[[Category: Weigelt, J.]]
[[Category: Weigelt J]]
[[Category: Xue, S.]]
[[Category: Xue S]]
[[Category: E3 ligase]]
[[Category: Ligase]]
[[Category: Protein ubiquitination]]
[[Category: Sgc]]
[[Category: Structural genomic]]
[[Category: Structural genomics consortium]]