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[[Image:2vm6.jpg|left|200px]]<br /><applet load="2vm6" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2vm6, resolution 2.20&Aring;" />
'''HUMAN BCL2-A1 IN COMPLEX WITH BIM-BH3 PEPTIDE'''<br />


==About this Structure==
==Human Bcl2-A1 in complex with Bim-BH3 peptide==
2VM6 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:So4+Binding+Site+For+Residue+A+1150'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VM6 OCA].  
<StructureSection load='2vm6' size='340' side='right'caption='[[2vm6]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2vm6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VM6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VM6 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2vm6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vm6 OCA], [https://pdbe.org/2vm6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vm6 RCSB], [https://www.ebi.ac.uk/pdbsum/2vm6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vm6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B2LA1_HUMAN B2LA1_HUMAN] 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 (By similarity).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vm/2vm6_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2vm6 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Evasion of apoptosis is recognized as a characteristic of malignant growth. Anti-apoptotic B-cell lymphoma-2 (Bcl-2) family members have therefore emerged as potential therapeutic targets due to their critical role in proliferating cancer cells. Here, we present the crystal structure of Bfl-1, the last anti-apoptotic Bcl-2 family member to be structurally characterized, in complex with a peptide corresponding to the BH3 region of the pro-apoptotic protein Bim. The structure reveals distinct features at the peptide-binding site, likely to define the binding specificity for pro-apoptotic proteins. Superposition of the Bfl-1:Bim complex with that of Mcl-1:Bim reveals a significant local plasticity of hydrophobic interactions contributed by the Bim peptide, likely to be the basis for the multi specificity of Bim for anti-apoptotic proteins.
 
Completing the family portrait of the anti-apoptotic Bcl-2 proteins: crystal structure of human Bfl-1 in complex with Bim.,Herman MD, Nyman T, Welin M, Lehtio L, Flodin S, Tresaugues L, Kotenyova T, Flores A, Nordlund P FEBS Lett. 2008 Oct 29;582(25-26):3590-4. Epub 2008 Sep 21. PMID:18812174<ref>PMID:18812174</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2vm6" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[B-cell lymphoma proteins 3D structures|B-cell lymphoma proteins 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C.H.]]
[[Category: Arrowsmith CH]]
[[Category: Berg, S.Van.Den.]]
[[Category: Berglund H]]
[[Category: Berglund, H.]]
[[Category: Busam RD]]
[[Category: Busam, R.D.]]
[[Category: Collins R]]
[[Category: Collins, R.]]
[[Category: Dahlgren LG]]
[[Category: Dahlgren, L.G.]]
[[Category: Edwards AM]]
[[Category: Edwards, A.M.]]
[[Category: Flodin S]]
[[Category: Flodin, S.]]
[[Category: Flores A]]
[[Category: Flores, A.]]
[[Category: Graslund S]]
[[Category: Graslund, S.]]
[[Category: Hammarstrom M]]
[[Category: Hammarstrom, M.]]
[[Category: Herman MD]]
[[Category: Herman, M.D.]]
[[Category: Johansson I]]
[[Category: Johansson, I.]]
[[Category: Kallas A]]
[[Category: Kallas, A.]]
[[Category: Karlberg T]]
[[Category: Karlberg, T.]]
[[Category: Kotenyova T]]
[[Category: Kotenyova, T.]]
[[Category: Lehtio L]]
[[Category: Lehtio, L.]]
[[Category: Moche M]]
[[Category: Moche, M.]]
[[Category: Nilsson ME]]
[[Category: Nilsson, M.E.]]
[[Category: Nordlund P]]
[[Category: Nordlund, P.]]
[[Category: Nyman T]]
[[Category: Nyman, T.]]
[[Category: Persson C]]
[[Category: Persson, C.]]
[[Category: Sagemark J]]
[[Category: Sagemark, J.]]
[[Category: Svensson L]]
[[Category: Sgc, Structural.Genomics.Consortium.]]
[[Category: Thorsell AG]]
[[Category: Svensson, L.]]
[[Category: Tresaugues L]]
[[Category: Thorsell, A.G.]]
[[Category: Weigelt J]]
[[Category: Tresaugues, L.]]
[[Category: Welin M]]
[[Category: Weigelt, J.]]
[[Category: Van den Berg S]]
[[Category: Welin, M.]]
[[Category: SO4]]
[[Category: alternative splicing]]
[[Category: antiapoptotic]]
[[Category: apoptosis]]
[[Category: b-cell lymphoma2]]
[[Category: bcl-2a1]]
[[Category: bcl2a1]]
[[Category: bfl-1]]
[[Category: bim]]
[[Category: cytoplasm]]
[[Category: immune system]]
[[Category: membrane]]
[[Category: polymorphism]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb  6 17:24:50 2008''

Latest revision as of 13:01, 9 May 2024

Human Bcl2-A1 in complex with Bim-BH3 peptideHuman Bcl2-A1 in complex with Bim-BH3 peptide

Structural highlights

2vm6 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

B2LA1_HUMAN 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 (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

Evasion of apoptosis is recognized as a characteristic of malignant growth. Anti-apoptotic B-cell lymphoma-2 (Bcl-2) family members have therefore emerged as potential therapeutic targets due to their critical role in proliferating cancer cells. Here, we present the crystal structure of Bfl-1, the last anti-apoptotic Bcl-2 family member to be structurally characterized, in complex with a peptide corresponding to the BH3 region of the pro-apoptotic protein Bim. The structure reveals distinct features at the peptide-binding site, likely to define the binding specificity for pro-apoptotic proteins. Superposition of the Bfl-1:Bim complex with that of Mcl-1:Bim reveals a significant local plasticity of hydrophobic interactions contributed by the Bim peptide, likely to be the basis for the multi specificity of Bim for anti-apoptotic proteins.

Completing the family portrait of the anti-apoptotic Bcl-2 proteins: crystal structure of human Bfl-1 in complex with Bim.,Herman MD, Nyman T, Welin M, Lehtio L, Flodin S, Tresaugues L, Kotenyova T, Flores A, Nordlund P FEBS Lett. 2008 Oct 29;582(25-26):3590-4. Epub 2008 Sep 21. PMID:18812174[1]

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

See Also

References

  1. ↑ Herman MD, Nyman T, Welin M, Lehtio L, Flodin S, Tresaugues L, Kotenyova T, Flores A, Nordlund P. Completing the family portrait of the anti-apoptotic Bcl-2 proteins: crystal structure of human Bfl-1 in complex with Bim. FEBS Lett. 2008 Oct 29;582(25-26):3590-4. Epub 2008 Sep 21. PMID:18812174 doi:S0014-5793(08)00763-1

2vm6, resolution 2.20Å

Drag the structure with the mouse to rotate

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