1maz

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[[Image:1maz.jpg|left|200px]]<br /><applet load="1maz" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1maz, resolution 2.2&Aring;" />
 
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'''X-RAY STRUCTURE OF BCL-XL, AN INHIBITOR OF PROGRAMMED CELL DEATH'''<br />
 
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==Overview==
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==X-RAY STRUCTURE OF BCL-XL, AN INHIBITOR OF PROGRAMMED CELL DEATH==
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THE Bcl-2 family of proteins regulate programmed cell death by an unknown, mechanism. Here we describe the crystal and solution structures of a Bcl-2, family member, Bcl-xL (ref. 2). The structures consist of two central, primarily hydrophobic alpha-helices, which are surrounded by amphipathic, helices. A 60-residue loop connecting helices alpha1 and alpha2 was found, to be flexible and non-essential for anti-apoptotic activity. The three, functionally important Bcl-2 homology regions (BH1, BH2 and BH3) are in, close spatial proximity and form an elongated hydrophobic cleft that may, represent the binding site for other Bcl-2 family members. The arrangement, of the alpha-helices in Bcl-xL is reminiscent of the membrane, translocation domain of bacterial toxins, in particular diphtheria toxin, and the colicins. The structural similarity may provide a clue to the, mechanism of action of the Bcl-2 family of proteins.
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<StructureSection load='1maz' size='340' side='right'caption='[[1maz]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1maz]] 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=1MAZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MAZ FirstGlance]. <br>
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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]] 2.2&#8491;</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=1maz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1maz OCA], [https://pdbe.org/1maz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1maz RCSB], [https://www.ebi.ac.uk/pdbsum/1maz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1maz ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/B2CL1_HUMAN B2CL1_HUMAN] Potent inhibitor of cell death. Inhibits activation of caspases (By similarity). Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis.<ref>PMID:19917720</ref> <ref>PMID:21840391</ref> Isoform Bcl-X(S) promotes apoptosis.<ref>PMID:19917720</ref> <ref>PMID:21840391</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/ma/1maz_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=1maz ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1MAZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MAZ OCA].
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*[[B-cell lymphoma proteins 3D structures|B-cell lymphoma proteins 3D structures]]
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== References ==
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==Reference==
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<references/>
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X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death., Muchmore SW, Sattler M, Liang H, Meadows RP, Harlan JE, Yoon HS, Nettesheim D, Chang BS, Thompson CB, Wong SL, Ng SL, Fesik SW, Nature. 1996 May 23;381(6580):335-41. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8692274 8692274]
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__TOC__
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[[Category: Escherichia coli]]
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</StructureSection>
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[[Category: Single protein]]
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[[Category: Homo sapiens]]
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[[Category: Chang, B.S.]]
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[[Category: Large Structures]]
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[[Category: Fesik, S.W.]]
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[[Category: Chang BS]]
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[[Category: Harlan, J.E.]]
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[[Category: Fesik SW]]
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[[Category: Liang, H.]]
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[[Category: Harlan JE]]
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[[Category: Meadows, R.P.]]
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[[Category: Liang H]]
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[[Category: Muchmore, S.W.]]
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[[Category: Meadows RP]]
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[[Category: Nettesheim, D.]]
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[[Category: Muchmore SW]]
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[[Category: Ng, S.C.]]
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[[Category: Nettesheim D]]
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[[Category: Sattler, M.]]
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[[Category: Ng SC]]
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[[Category: Thompson, C.B.]]
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[[Category: Sattler M]]
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[[Category: Wong, S.L.]]
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[[Category: Thompson CB]]
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[[Category: Yoon, H.S.]]
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[[Category: Wong SL]]
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[[Category: apoptosis]]
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[[Category: Yoon HS]]
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[[Category: bcl-2 family]]
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[[Category: programmed cell death]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:23:26 2008''
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X-RAY STRUCTURE OF BCL-XL, AN INHIBITOR OF PROGRAMMED CELL DEATH

PDB ID 1maz

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