2vof

From Proteopedia

(Difference between revisions)

Revision as of 20:08, 25 December 2014

STRUCTURE OF MOUSE A1 BOUND TO THE PUMA BH3-DOMAIN

Structural highlights

2vof is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	2vog, 2voh, 2voi
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[BBC3_MOUSE] Essential mediator of p53/TP53-dependent and p53/TP53-independent apoptosis (By similarity). Regulates ER stress-induced neuronal apoptosis.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Apoptotic pathways are regulated by protein-protein interactions. Interaction of the BH3 domains of proapoptotic Bcl-2 family proteins with the hydrophobic groove of prosurvival proteins is critical. Whereas some BH3 domains bind in a promiscuous manner, others exhibit considerable selectivity and the sequence characteristics that distinguish these activities are unclear. In this study, crystal structures of complexes between the prosurvival protein A1 and the BH3 domains from Puma, Bmf, Bak, and Bid have been solved. The structure of A1 is similar to that of other prosurvival proteins, although features, such as an acidic patch in the binding groove, may allow specific therapeutic modulation of apoptosis. Significant conformational plasticity was observed in the intermolecular interactions and these differences explain some of the variation in affinity. This study, in combination with published data, suggests that interactions between conserved residues demarcate optimal binding.

Structural plasticity underpins promiscuous binding of the prosurvival protein A1.,Smits C, Czabotar PE, Hinds MG, Day CL Structure. 2008 May;16(5):818-29. PMID:18462686^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Galehdar Z, Swan P, Fuerth B, Callaghan SM, Park DS, Cregan SP. Neuronal apoptosis induced by endoplasmic reticulum stress is regulated by ATF4-CHOP-mediated induction of the Bcl-2 homology 3-only member PUMA. J Neurosci. 2010 Dec 15;30(50):16938-48. doi: 10.1523/JNEUROSCI.1598-10.2010. PMID:21159964 doi:http://dx.doi.org/10.1523/JNEUROSCI.1598-10.2010
↑ Ghosh AP, Klocke BJ, Ballestas ME, Roth KA. CHOP potentially co-operates with FOXO3a in neuronal cells to regulate PUMA and BIM expression in response to ER stress. PLoS One. 2012;7(6):e39586. doi: 10.1371/journal.pone.0039586. Epub 2012 Jun 28. PMID:22761832 doi:http://dx.doi.org/10.1371/journal.pone.0039586
↑ Smits C, Czabotar PE, Hinds MG, Day CL. Structural plasticity underpins promiscuous binding of the prosurvival protein A1. Structure. 2008 May;16(5):818-29. PMID:18462686 doi:http://dx.doi.org/10.1016/j.str.2008.02.009

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2vof"

@@ Line 2: / Line 2: @@
 <StructureSection load='2vof' size='340' side='right' caption='[[2vof]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2vof]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VOF OCA]. <br>
+<table><tr><td colspan='2'>[[2vof]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VOF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VOF FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene><br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
-<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vog|2vog]], [[2voh|2voh]], [[2voi|2voi]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vog|2vog]], [[2voh|2voh]], [[2voi|2voi]]</td></tr>
-<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vof OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vof RCSB], [http://www.ebi.ac.uk/pdbsum/2vof PDBsum]</span></td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vof OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vof RCSB], [http://www.ebi.ac.uk/pdbsum/2vof PDBsum]</span></td></tr>
+</table>
-<table>
+== Function ==
+[[http://www.uniprot.org/uniprot/BBC3_MOUSE BBC3_MOUSE]] Essential mediator of p53/TP53-dependent and p53/TP53-independent apoptosis (By similarity). Regulates ER stress-induced neuronal apoptosis.<ref>PMID:21159964</ref> <ref>PMID:22761832</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 25: / Line 26: @@
 Structural plasticity underpins promiscuous binding of the prosurvival protein A1.,Smits C, Czabotar PE, Hinds MG, Day CL Structure. 2008 May;16(5):818-29. PMID:18462686<ref>PMID:18462686</ref>
-From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
 == References ==
@@ Line 32: / Line 33: @@
 </StructureSection>
 [[Category: Mus musculus]]
-[[Category: Czabotar, P E.]]
+[[Category: Czabotar, P E]]
-[[Category: Day, C L.]]
+[[Category: Day, C L]]
-[[Category: Hinds, M G.]]
+[[Category: Hinds, M G]]
-[[Category: Smits, C.]]
+[[Category: Smits, C]]
 [[Category: Apoptosis]]
 [[Category: Bcl-2]]

2vof

From Proteopedia

Revision as of 20:08, 25 December 2014

STRUCTURE OF MOUSE A1 BOUND TO THE PUMA BH3-DOMAIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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