1af3
From Proteopedia
(Difference between revisions)
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<StructureSection load='1af3' size='340' side='right'caption='[[1af3]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1af3' size='340' side='right'caption='[[1af3]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1af3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1af3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AF3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AF3 FirstGlance]. <br> |
| - | </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=1af3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1af3 OCA], [https://pdbe.org/1af3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1af3 RCSB], [https://www.ebi.ac.uk/pdbsum/1af3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1af3 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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=1af3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1af3 OCA], [https://pdbe.org/1af3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1af3 RCSB], [https://www.ebi.ac.uk/pdbsum/1af3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1af3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/B2CL1_RAT B2CL1_RAT] 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:8662675</ref> <ref>PMID:7828536</ref> <ref>PMID:18250306</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=1af3 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=1af3 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Bcl-xL is a member of the Bcl-2 protein family, which regulates apoptosis. Preparation of recombinant rat Bcl-xL yielded two forms, one deamidated at -Asn-Gly- sequences to produce isoaspartates and the other not deamidated. The crystal structures of the two forms show that they both adopt an essentially identical backbone structure which resembles the fold of human Bcl-xL: three layers of two alpha-helices each, capped at one end by two short helices. Both forms have a long disordered region, which contains the potential deamidation sites. The molecular structure exhibits a low level of interhelical interactions, the presence of three cavities, and a notable hydrophobic cleft surrounded by walls rich in basic residues. These unique structural features may be favorable for its accommodation into membranes or for possible rearrangement to modulate homo-/heterodimerization. Homology modeling of Bcl-2 and Bax, based on the Bcl-xL structure, suggests that Bax has the strongest potential for membrane insertion. Furthermore, we found a possible interface for interaction with non-Bcl-2 family member proteins, such as CED-4 homologues. | ||
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| - | Crystal structure of rat Bcl-xL. Implications for the function of the Bcl-2 protein family.,Aritomi M, Kunishima N, Inohara N, Ishibashi Y, Ohta S, Morikawa K J Biol Chem. 1997 Oct 31;272(44):27886-92. PMID:9346936<ref>PMID:9346936</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1af3" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Buffalo rat]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Aritomi | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Inohara | + | [[Category: Aritomi M]] |
| - | [[Category: Ishibashi | + | [[Category: Inohara N]] |
| - | [[Category: Kunishima | + | [[Category: Ishibashi Y]] |
| - | [[Category: Morikawa | + | [[Category: Kunishima N]] |
| - | [[Category: Ohta | + | [[Category: Morikawa K]] |
| - | + | [[Category: Ohta S]] | |
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Current revision
RAT BCL-XL AN APOPTOSIS INHIBITORY PROTEIN
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