View source for 6rjp


==Bfl-1 in complex with alpha helical peptide==
<StructureSection load='6rjp' size='340' side='right'caption='[[6rjp]], [[Resolution|resolution]] 2.57&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
== 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).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6rjp" 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: Large Structures]]
[[Category: Baggio C]]
[[Category: Gambini L]]
[[Category: Hakansson M]]
[[Category: Jossart J]]
[[Category: Pellecchia M]]
[[Category: Perry J]]
[[Category: Salem AF]]
[[Category: Udompholkul P]]