1f16

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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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<StructureSection load='1f16' size='340' side='right' caption='[[1f16]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1f16]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F16 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f16 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1f16 RCSB], [http://www.ebi.ac.uk/pdbsum/1f16 PDBsum]</span></td></tr>
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<table>
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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/chain_selection.php?pdb_ID=2ata 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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{{STRUCTURE_1f16| PDB=1f16 | SCENE= }}
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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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===SOLUTION STRUCTURE OF A PRO-APOPTOTIC PROTEIN BAX===
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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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== References ==
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==About this Structure==
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<references/>
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[[1f16]] is a 1 chain structure with 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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__TOC__
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:011106734</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Suzuki, M.]]
[[Category: Suzuki, M.]]

Revision as of 13:06, 28 September 2014

SOLUTION STRUCTURE OF A PRO-APOPTOTIC PROTEIN BAX

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