3h13: Difference between revisions

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New page: '''Unreleased structure''' The entry 3h13 is ON HOLD Authors: Jeffrey, P.D., Yu, J.W., Shi, Y. Description: c-FLIPL protease-like domain ''Page seeded by [http://oca.weizmann.ac.il/oc...
 
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'''Unreleased structure'''


The entry 3h13 is ON HOLD
==c-FLIPL protease-like domain==
 
<StructureSection load='3h13' size='340' side='right'caption='[[3h13]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
Authors: Jeffrey, P.D., Yu, J.W., Shi, Y.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[3h13]] 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=3H13 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H13 FirstGlance]. <br>
Description: c-FLIPL protease-like domain
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#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=3h13 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h13 OCA], [https://pdbe.org/3h13 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h13 RCSB], [https://www.ebi.ac.uk/pdbsum/3h13 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h13 ProSAT]</span></td></tr>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 22 11:09:38 2009''
</table>
== Function ==
[https://www.uniprot.org/uniprot/CFLAR_HUMAN CFLAR_HUMAN] Apoptosis regulator protein which may function as a crucial link between cell survival and cell death pathways in mammalian cells. Acts as an inhibitor of TNFRSF6 mediated apoptosis. A proteolytic fragment (p43) is likely retained in the death-inducing signaling complex (DISC) thereby blocking further recruitment and processing of caspase-8 at the complex. Full length and shorter isoforms have been shown either to induce apoptosis or to reduce TNFRSF-triggered apoptosis. Lacks enzymatic (caspase) activity.<ref>PMID:9880531</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/h1/3h13_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=3h13 ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Jeffrey PD]]
[[Category: Shi Y]]
[[Category: Yu JW]]

Latest revision as of 09:57, 21 February 2024

c-FLIPL protease-like domain

3h13, resolution 2.20Å

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