1maz
From Proteopedia
(Difference between revisions)
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<StructureSection load='1maz' size='340' side='right'caption='[[1maz]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1maz' size='340' side='right'caption='[[1maz]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1maz]] is a 1 chain structure with sequence from [ | + | <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> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | + | <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> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [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> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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]. | </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]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == 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. | ||
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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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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1maz" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Chang | + | [[Category: Chang BS]] |
| - | [[Category: Fesik | + | [[Category: Fesik SW]] |
| - | [[Category: Harlan | + | [[Category: Harlan JE]] |
| - | [[Category: Liang | + | [[Category: Liang H]] |
| - | [[Category: Meadows | + | [[Category: Meadows RP]] |
| - | [[Category: Muchmore | + | [[Category: Muchmore SW]] |
| - | [[Category: Nettesheim | + | [[Category: Nettesheim D]] |
| - | [[Category: Ng | + | [[Category: Ng SC]] |
| - | [[Category: Sattler | + | [[Category: Sattler M]] |
| - | [[Category: Thompson | + | [[Category: Thompson CB]] |
| - | [[Category: Wong | + | [[Category: Wong SL]] |
| - | [[Category: Yoon | + | [[Category: Yoon HS]] |
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Current revision
X-RAY STRUCTURE OF BCL-XL, AN INHIBITOR OF PROGRAMMED CELL DEATH
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Categories: Homo sapiens | Large Structures | Chang BS | Fesik SW | Harlan JE | Liang H | Meadows RP | Muchmore SW | Nettesheim D | Ng SC | Sattler M | Thompson CB | Wong SL | Yoon HS
