2vof: Difference between revisions

Revision as of 20:50, 19 September 2018

Structure of mouse A1 bound to the Puma BH3-domain

Structural highlights

2vof is a 4 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:	CL
NonStd Res:	MSE
Related:	2vog, 2voh, 2voi
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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:https://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:https://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:https://dx.doi.org/10.1016/j.str.2008.02.009

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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:https://dx.doi.org/10.1523/JNEUROSCI.1598-10.2010

[2] 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:https://dx.doi.org/10.1371/journal.pone.0039586

[3] 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:https://dx.doi.org/10.1016/j.str.2008.02.009

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@@ Line 1: / Line 1: @@
-==STRUCTURE OF MOUSE A1 BOUND TO THE PUMA BH3-DOMAIN==
+==Structure of mouse A1 bound to the Puma BH3-domain==
 <StructureSection load='2vof' size='340' side='right' caption='[[2vof]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
@@ Line 15: / Line 15: @@
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vo/2vof_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vo/2vof_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 30: / Line 30: @@
 </div>
 <div class="pdbe-citations 2vof" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[B-cell lymphoma protein|B-cell lymphoma protein]]
 == References ==
 <references/>

2vof: Difference between revisions

Revision as of 20:50, 19 September 2018

Structure of mouse A1 bound to the Puma BH3-domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

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