1maz
From Proteopedia
(Difference between revisions)
| (One intermediate revision not shown.) | |||
| Line 1: | Line 1: | ||
==X-RAY STRUCTURE OF BCL-XL, AN INHIBITOR OF PROGRAMMED CELL DEATH== | ==X-RAY STRUCTURE OF BCL-XL, AN INHIBITOR OF PROGRAMMED CELL DEATH== | ||
| - | <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]] | ||
| Line 20: | Line 19: | ||
</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. | ||
| - | + | ==See Also== | |
| - | + | *[[B-cell lymphoma proteins 3D structures|B-cell lymphoma proteins 3D structures]] | |
| - | + | ||
| - | + | ||
| - | + | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | [[Category: Chang | + | [[Category: Large Structures]] |
| - | [[Category: Fesik | + | [[Category: Chang BS]] |
| - | [[Category: Harlan | + | [[Category: Fesik SW]] |
| - | [[Category: Liang | + | [[Category: Harlan JE]] |
| - | [[Category: Meadows | + | [[Category: Liang H]] |
| - | [[Category: Muchmore | + | [[Category: Meadows RP]] |
| - | [[Category: Nettesheim | + | [[Category: Muchmore SW]] |
| - | [[Category: Ng | + | [[Category: Nettesheim D]] |
| - | [[Category: Sattler | + | [[Category: Ng SC]] |
| - | [[Category: Thompson | + | [[Category: Sattler M]] |
| - | [[Category: Wong | + | [[Category: Thompson CB]] |
| - | [[Category: Yoon | + | [[Category: Wong SL]] |
| - | + | [[Category: Yoon HS]] | |
| - | + | ||
| - | + | ||
Current revision
X-RAY STRUCTURE OF BCL-XL, AN INHIBITOR OF PROGRAMMED CELL DEATH
| |||||||||||
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
