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- | [[Image:1ohu.jpg|left|200px]] | |
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- | <!--
| + | ==Structure of Caenorhabditis elegans CED-9== |
- | The line below this paragraph, containing "STRUCTURE_1ohu", creates the "Structure Box" on the page.
| + | <StructureSection load='1ohu' size='340' side='right'caption='[[1ohu]], [[Resolution|resolution]] 2.03Å' scene=''> |
- | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
- | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <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> |
- | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.03Å</td></tr> |
- | --> | + | <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> |
- | {{STRUCTURE_1ohu| PDB=1ohu | SCENE= }}
| + | <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> |
| + | </table> |
| + | == Function == |
| + | [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> |
| + | == 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/oh/1ohu_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=1ohu ConSurf]. |
| + | <div style="clear:both"></div> |
| | | |
- | '''STRUCTURE OF CAENORHABDITIS ELEGANS CED-9'''
| + | ==See Also== |
- | | + | *[[Cell death protein 3D structures|Cell death protein 3D structures]] |
- | | + | == References == |
- | ==Overview== | + | <references/> |
- | 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.
| + | __TOC__ |
- | | + | </StructureSection> |
- | ==About this Structure==
| + | |
- | 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].
| + | |
- | | + | |
- | ==Reference== | + | |
- | 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]] |
- | [[Category: Single protein]] | + | [[Category: Large Structures]] |
- | [[Category: Ha, N C.]] | + | [[Category: Ha N-C]] |
- | [[Category: Jeong, J S.]] | + | [[Category: Jeong J-S]] |
- | [[Category: Oh, B H.]] | + | [[Category: Oh B-H]] |
- | [[Category: Apoptosis]]
| + | |
- | [[Category: Bcl-2 family]]
| + | |
- | [[Category: Ced-9]]
| + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:52:00 2008''
| + | |
| Structural highlights
Function
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.[1] [2] [3] [4] [5] [6]
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
- ↑ Hengartner MO, Horvitz HR. C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2. Cell. 1994 Feb 25;76(4):665-76. PMID:7907274
- ↑ Spector MS, Desnoyers S, Hoeppner DJ, Hengartner MO. Interaction between the C. elegans cell-death regulators CED-9 and CED-4. Nature. 1997 Feb 13;385(6617):653-6. PMID:9024666 doi:http://dx.doi.org/10.1038/385653a0
- ↑ Wu D, Wallen HD, Nunez G. Interaction and regulation of subcellular localization of CED-4 by CED-9. Science. 1997 Feb 21;275(5303):1126-9. PMID:9027313
- ↑ Conradt B, Horvitz HR. The C. elegans protein EGL-1 is required for programmed cell death and interacts with the Bcl-2-like protein CED-9. Cell. 1998 May 15;93(4):519-29. PMID:9604928
- ↑ Chen F, Hersh BM, Conradt B, Zhou Z, Riemer D, Gruenbaum Y, Horvitz HR. Translocation of C. elegans CED-4 to nuclear membranes during programmed cell death. Science. 2000 Feb 25;287(5457):1485-9. PMID:10688797
- ↑ Yan N, Gu L, Kokel D, Chai J, Li W, Han A, Chen L, Xue D, Shi Y. Structural, biochemical, and functional analyses of CED-9 recognition by the proapoptotic proteins EGL-1 and CED-4. Mol Cell. 2004 Sep 24;15(6):999-1006. PMID:15383288 doi:10.1016/j.molcel.2004.08.022
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