1ohu

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[[Image:1ohu.jpg|left|200px]]
 
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{{Structure
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==Structure of Caenorhabditis elegans CED-9==
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|PDB= 1ohu |SIZE=350|CAPTION= <scene name='initialview01'>1ohu</scene>, resolution 2.03&Aring;
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<StructureSection load='1ohu' size='340' side='right'caption='[[1ohu]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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<table><tr><td colspan='2'>[[1ohu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OHU FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.03&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ohu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ohu OCA], [https://pdbe.org/1ohu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ohu RCSB], [https://www.ebi.ac.uk/pdbsum/1ohu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ohu ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ohu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ohu OCA], [http://www.ebi.ac.uk/pdbsum/1ohu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ohu RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/CED9_CAEEL CED9_CAEEL] Plays a major role in programmed cell death (PCD, apoptosis). Egl-1 binds to and directly inhibits the activity of ced-9, releasing the cell death activator ced-4 from a ced-9/ced-4 containing protein complex and allowing ced-4 to activate the cell-killing caspase ced-3.<ref>PMID:7907274</ref> <ref>PMID:9024666</ref> <ref>PMID:9027313</ref> <ref>PMID:9604928</ref> <ref>PMID:10688797</ref> <ref>PMID:15383288</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oh/1ohu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1ohu ConSurf].
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<div style="clear:both"></div>
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'''STRUCTURE OF CAENORHABDITIS ELEGANS CED-9'''
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==See Also==
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*[[Cell death protein 3D structures|Cell death protein 3D structures]]
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== References ==
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==Overview==
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<references/>
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The interactions between B-cell lymphoma 2 (BCL-2) family members are known to be mediated through the binding of the BH3 domain of a proapoptotic member to the BH3-binding groove of an antiapoptotic member. We determined the crystal structure of antiapoptotic CED-9, which reveals a unique C-terminal helix altering the common BH3-binding region. A coexpression system to produce CED-9 in complex with proapoptotic EGL-1 enabled us to show that the binding of EGL-1 to CED-9 is extremely stable, raising the melting temperature (T(M)) of CED-9 by 25 degrees C, and that the binding surface of CED-9 extends beyond the BH3-binding region and reaches the BH4 domain. Consistently, the T(M) and a 1H-15N correlation NMR spectrum of CED-9 in complex with EGL-1 are drastically different from those of CED-9 in complex with the EGL-1 BH3 peptide. The data suggest that the recognition between other BCL-2 family members may also involve much wider protein surfaces than is previously thought.
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__TOC__
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</StructureSection>
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==About this Structure==
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1OHU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OHU OCA].
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==Reference==
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Unique structural features of a BCL-2 family protein CED-9 and biophysical characterization of CED-9/EGL-1 interactions., Woo JS, Jung JS, Ha NC, Shin J, Kim KH, Lee W, Oh BH, Cell Death Differ. 2003 Dec;10(12):1310-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12894216 12894216]
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[[Category: Caenorhabditis elegans]]
[[Category: Caenorhabditis elegans]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Ha, N C.]]
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[[Category: Ha N-C]]
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[[Category: Jeong, J S.]]
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[[Category: Jeong J-S]]
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[[Category: Oh, B H.]]
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[[Category: Oh B-H]]
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[[Category: apoptosis]]
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[[Category: bcl-2 family]]
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[[Category: ced-9]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:45:37 2008''
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Current revision

Structure of Caenorhabditis elegans CED-9

PDB ID 1ohu

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