1lxl

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[[Image:1lxl.gif|left|200px]]
 
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{{Structure
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==NMR STRUCTURE OF BCL-XL, AN INHIBITOR OF PROGRAMMED CELL DEATH, MINIMIZED AVERAGE STRUCTURE==
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|PDB= 1lxl |SIZE=350|CAPTION= <scene name='initialview01'>1lxl</scene>
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<StructureSection load='1lxl' size='340' side='right'caption='[[1lxl]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1lxl]] 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=1LXL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LXL 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">Solution NMR</td></tr>
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|GENE= HUMAN BCL-XL RESIDUES 1-209 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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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=1lxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lxl OCA], [https://pdbe.org/1lxl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lxl RCSB], [https://www.ebi.ac.uk/pdbsum/1lxl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lxl ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lxl OCA], [http://www.ebi.ac.uk/pdbsum/1lxl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lxl RCSB]</span>
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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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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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'''NMR STRUCTURE OF BCL-XL, AN INHIBITOR OF PROGRAMMED CELL DEATH, MINIMIZED AVERAGE STRUCTURE'''
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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/lx/1lxl_consurf.spt"</scriptWhenChecked>
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==Overview==
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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=1lxl 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 ==
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.
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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==About this Structure==
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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:8692274<ref>PMID:8692274</ref>
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1LXL is a [[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=1LXL OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://www.ncbi.nlm.nih.gov/pubmed/8692274 8692274]
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</div>
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[[Category: Escherichia coli]]
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<div class="pdbe-citations 1lxl" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Chang, B S.]]
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[[Category: Fesik, S W.]]
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[[Category: Harlan, J E.]]
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[[Category: Liang, H.]]
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[[Category: Meadows, R P.]]
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[[Category: Muchmore, S W.]]
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[[Category: Nettesheim, D.]]
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[[Category: Ng, S C.]]
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[[Category: Sattler, M.]]
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[[Category: Thompson, C B.]]
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[[Category: Wong, S L.]]
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[[Category: Yoon, H S.]]
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[[Category: apoptosis]]
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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 Sun Mar 30 22:08:40 2008''
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==See Also==
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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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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Chang BS]]
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[[Category: Fesik SW]]
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[[Category: Harlan JE]]
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[[Category: Liang H]]
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[[Category: Meadows RP]]
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[[Category: Muchmore SW]]
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[[Category: Nettesheim D]]
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[[Category: Ng SC]]
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[[Category: Sattler M]]
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[[Category: Thompson CB]]
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[[Category: Wong SL]]
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[[Category: Yoon HS]]

Current revision

NMR STRUCTURE OF BCL-XL, AN INHIBITOR OF PROGRAMMED CELL DEATH, MINIMIZED AVERAGE STRUCTURE

PDB ID 1lxl

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