1f16

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{{Seed}}
 
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[[Image:1f16.png|left|200px]]
 
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==SOLUTION STRUCTURE OF A PRO-APOPTOTIC PROTEIN BAX==
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The line below this paragraph, containing "STRUCTURE_1f16", creates the "Structure Box" on the page.
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<StructureSection load='1f16' size='340' side='right'caption='[[1f16]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1f16]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F16 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F16 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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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=1f16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f16 OCA], [https://pdbe.org/1f16 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f16 RCSB], [https://www.ebi.ac.uk/pdbsum/1f16 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f16 ProSAT]</span></td></tr>
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{{STRUCTURE_1f16| PDB=1f16 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BAX_HUMAN BAX_HUMAN] Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis.<ref>PMID:8358790</ref> <ref>PMID:10772918</ref> <ref>PMID:8521816</ref> <ref>PMID:16113678</ref> <ref>PMID:18948948</ref> <ref>PMID:21199865</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/f1/1f16_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=1f16 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Apoptosis is stimulated by the insertion of Bax from the cytosol into mitochondrial membranes. The solution structure of Bax, including the putative transmembrane domain at the C terminus, was determined in order to understand the regulation of its subcellular location. Bax consists of 9 alpha helices where the assembly of helices alpha1 through alpha 8 resembles that of the apoptosis inhibitor, Bcl-x(L). The C-terminal alpha 9 helix occupies the hydrophobic pocket proposed previously to mediate heterodimer formation and bioactivity of opposing members of the Bcl-2 family. The Bax structure shows that the orientation of helix alpha 9 provides simultaneous control over its mitochondrial targeting and dimer formation.
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===SOLUTION STRUCTURE OF A PRO-APOPTOTIC PROTEIN BAX===
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Structure of Bax: coregulation of dimer formation and intracellular localization.,Suzuki M, Youle RJ, Tjandra N Cell. 2000 Nov 10;103(4):645-54. PMID:11106734<ref>PMID:11106734</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_11106734}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1f16" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 11106734 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11106734}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1F16 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F16 OCA].
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==Reference==
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<ref group="xtra">PMID:11106734</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Suzuki, M.]]
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[[Category: Large Structures]]
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[[Category: Tjandra, N.]]
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[[Category: Suzuki M]]
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[[Category: Youle, R J.]]
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[[Category: Tjandra N]]
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[[Category: Helical protein]]
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[[Category: Youle RJ]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 13:30:11 2009''
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Current revision

SOLUTION STRUCTURE OF A PRO-APOPTOTIC PROTEIN BAX

PDB ID 1f16

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