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2voh

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Revision as of 11:42, 30 March 2022

Structure of mouse A1 bound to the Bak BH3-domain

Structural highlights

2voh is a 2 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	2vof, 2vog, 2voi
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[BAK_MOUSE] In the presence of an appropriate stimulus, accelerates programmed cell death by binding to, and antagonizing the anti-apoptotic action of BCL2 (By similarity).

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^[1]

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

References

↑ 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 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <StructureSection load='2voh' size='340' side='right'caption='[[2voh]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2voh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VOH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VOH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2voh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VOH FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vof|2vof]], [[2vog|2vog]], [[2voi|2voi]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2vof|2vof]], [[2vog|2vog]], [[2voi|2voi]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2voh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2voh OCA], [http://pdbe.org/2voh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2voh RCSB], [http://www.ebi.ac.uk/pdbsum/2voh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2voh ProSAT]</span></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=2voh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2voh OCA], [https://pdbe.org/2voh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2voh RCSB], [https://www.ebi.ac.uk/pdbsum/2voh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2voh ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/BAK_MOUSE BAK_MOUSE]] In the presence of an appropriate stimulus, accelerates programmed cell death by binding to, and antagonizing the anti-apoptotic action of BCL2 (By similarity).
+[[https://www.uniprot.org/uniprot/BAK_MOUSE BAK_MOUSE]] In the presence of an appropriate stimulus, accelerates programmed cell death by binding to, and antagonizing the anti-apoptotic action of BCL2 (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2voh

From Proteopedia

Revision as of 11:42, 30 March 2022

Structure of mouse A1 bound to the Bak BH3-domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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