2vof

From Proteopedia

(Difference between revisions)

Current revision

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.
Method:	X-ray diffraction, Resolution 1.8Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

B2LA1_MOUSE Retards apoptosis induced by IL-3 deprivation. May function in the response of hemopoietic cells to external signals and in maintaining endothelial survival during infection. Can inhibit apoptosis induced by serum starvation in the mammary epithelial cell line HC11 (PubMed:11888890).^[1]

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^[2]

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

References

↑ Ha S, Lee S, Chung M, Choi Y. Mouse ING1 homologue, a protein interacting with A1, enhances cell death and is inhibited by A1 in mammary epithelial cells. Cancer Res. 2002 Mar 1;62(5):1275-8 PMID:11888890
↑ 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/2vof"

@@ Line 3: / Line 3: @@
 <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 [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=2VOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VOF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2vof]] is a 4 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2VOF FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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]] 1.8&#8491;</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 id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2vog|2vog]], [[2voh|2voh]], [[2voi|2voi]]</div></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=2vof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vof OCA], [https://pdbe.org/2vof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vof RCSB], [https://www.ebi.ac.uk/pdbsum/2vof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vof ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://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>
+[https://www.uniprot.org/uniprot/B2LA1_MOUSE B2LA1_MOUSE] Retards apoptosis induced by IL-3 deprivation. May function in the response of hemopoietic cells to external signals and in maintaining endothelial survival during infection. Can inhibit apoptosis induced by serum starvation in the mammary epithelial cell line HC11 (PubMed:11888890).<ref>PMID:11888890</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 16: / Line 15: @@
   <jmolCheckbox>
     <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>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 38: / Line 37: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Mus musculus]]
-[[Category: Czabotar, P E]]
+[[Category: Czabotar PE]]
-[[Category: Day, C L]]
+[[Category: Day CL]]
-[[Category: Hinds, M G]]
+[[Category: Hinds MG]]
-[[Category: Smits, C]]
+[[Category: Smits C]]
-[[Category: Apoptosis]]
-[[Category: Bcl-2]]
-[[Category: Bh3]]
-[[Category: Mitochondrion]]
-[[Category: Pro-survival]]
-[[Category: Protein-protein complex]]

2vof

From Proteopedia

Current revision

Structure of mouse A1 bound to the Puma BH3-domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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