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6rjp

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<StructureSection load='6rjp' size='340' side='right'caption='[[6rjp]], [[Resolution|resolution]] 2.57&Aring;' scene=''>
<StructureSection load='6rjp' size='340' side='right'caption='[[6rjp]], [[Resolution|resolution]] 2.57&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6rjp]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RJP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RJP FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6rjp]] is a 4 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=6RJP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RJP FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=AIB:ALPHA-AMINOISOBUTYRIC+ACID'>AIB</scene>, <scene name='pdbligand=LV8:'>LV8</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.57&#8491;</td></tr>
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<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=6rjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rjp OCA], [http://pdbe.org/6rjp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rjp RCSB], [http://www.ebi.ac.uk/pdbsum/6rjp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rjp ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AIB:ALPHA-AMINOISOBUTYRIC+ACID'>AIB</scene>, <scene name='pdbligand=LV8:(2~{S})-3-acetamido-2-azanyl-propanoic+acid'>LV8</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6rjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rjp OCA], [https://pdbe.org/6rjp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rjp RCSB], [https://www.ebi.ac.uk/pdbsum/6rjp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rjp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://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). [[http://www.uniprot.org/uniprot/B2L11_HUMAN B2L11_HUMAN]] Induces apoptosis and anoikis. Isoform BimL is more potent than isoform BimEL. Isoform Bim-alpha1, isoform Bim-alpha2 and isoform Bim-alpha3 induce apoptosis, although less potent than isoform BimEL, isoform BimL and isoform BimS. Isoform Bim-gamma induces apoptosis. Isoform Bim-alpha3 induces apoptosis possibly through a caspase-mediated pathway. Isoform BimAC and isoform BimABC lack the ability to induce apoptosis.<ref>PMID:9430630</ref> <ref>PMID:11734221</ref> <ref>PMID:12019181</ref> <ref>PMID:11997495</ref> <ref>PMID:15147734</ref> <ref>PMID:15486195</ref>
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[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).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Recently, it was reported that tetrapeptides cyclized via lactam bond between the amino terminus and a glutamic residue in position 4 (termed here N-lock) can nucleate helix formation in longer peptides. We applied such strategy to derive N-locked covalent BH3 peptides that were designed to selectively target the anti-apoptotic protein Bfl-1. The resulting agents were soluble in aqueous buffer and displayed a remarkable (low nanomolar) affinity for Bfl-1 and cellular activity. The crystal structure of the complex between such N-locked covalent peptide and Bfl-1 provided insights on the geometry of the N-locking strategy and of the covalent bond between the agent and Bfl-1.
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N-locking stabilization of covalent helical peptides: Application to Bfl-1 antagonists.,Baggio C, Udompholkul P, Gambini L, Jossart J, Salem AF, Hakansson M, Perry JJP, Pellecchia M Chem Biol Drug Des. 2020 Apr;95(4):412-426. doi: 10.1111/cbdd.13661. Epub 2020, Jan 20. PMID:31898401<ref>PMID:31898401</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6rjp" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[B-cell lymphoma proteins 3D structures|B-cell lymphoma proteins 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Baggio, C]]
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[[Category: Baggio C]]
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[[Category: Gambini, L]]
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[[Category: Gambini L]]
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[[Category: Hakansson, M]]
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[[Category: Hakansson M]]
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[[Category: Jossart, J]]
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[[Category: Jossart J]]
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[[Category: Pellecchia, M]]
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[[Category: Pellecchia M]]
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[[Category: Perry, J]]
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[[Category: Perry J]]
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[[Category: Salem, A F]]
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[[Category: Salem AF]]
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[[Category: Udompholkul, P]]
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[[Category: Udompholkul P]]
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[[Category: Bcl2-2 family protein]]
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[[Category: Covalent inhibitor]]
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[[Category: Peptide binding protein]]
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[[Category: Protein-protein interaction]]
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[[Category: Stapled alpha helix]]
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Current revision

Bfl-1 in complex with alpha helical peptide

PDB ID 6rjp

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