View source for 5agw


==Bcl-2 alpha beta-1 complex==
<StructureSection load='5agw' size='340' side='right'caption='[[5agw]], [[Resolution|resolution]] 2.69&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5agw]] 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=5AGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AGW 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]] 2.695&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=AJE:(3S,4R)-4-AMINO-1-(3-CARBOXYPROPANOYL)PYRROLIDINE-3-CARBOXYLIC+ACID'>AJE</scene>, <scene name='pdbligand=MH8:(2S)-2-AMINO-2-METHYLHEPT-6-ENOIC+ACID'>MH8</scene>, <scene name='pdbligand=XCP:(1S,2S)-2-AMINOCYCLOPENTANECARBOXYLIC+ACID'>XCP</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=5agw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5agw OCA], [https://pdbe.org/5agw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5agw RCSB], [https://www.ebi.ac.uk/pdbsum/5agw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5agw ProSAT]</span></td></tr>
</table>
== Function ==
[https://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> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Peptides can be developed as effective antagonists of protein-protein interactions, but conventional peptides (i.e., oligomers of l-alpha-amino acids) suffer from significant limitations in vivo. Short half-lives due to rapid proteolytic degradation and an inability to cross cell membranes often preclude biological applications of peptides. Oligomers that contain both alpha- and beta-amino acid residues ("alpha/beta-peptides") manifest decreased susceptibility to proteolytic degradation, and when properly designed these unnatural oligomers can mimic the protein-recognition properties of analogous "alpha-peptides". This report documents an extension of the alpha/beta-peptide approach to target intracellular protein-protein interactions. Specifically, we have generated alpha/beta-peptides based on a "stapled" Bim BH3 alpha-peptide, which contains a hydrocarbon cross-link to enhance alpha-helix stability. We show that a stapled alpha/beta-peptide can structurally and functionally mimic the parent stapled alpha-peptide in its ability to enter certain types of cells and block protein-protein interactions associated with apoptotic signaling. However, the alpha/beta-peptide is nearly 100-fold more resistant to proteolysis than is the parent stapled alpha-peptide. These results show that backbone modification, a strategy that has received relatively little attention in terms of peptide engineering for biomedical applications, can be combined with more commonly deployed peripheral modifications such as side chain cross-linking to produce synergistic benefits.

alpha/beta-Peptide Foldamers Targeting Intracellular Protein-Protein Interactions with Activity in Living Cells.,Checco JW, Lee EF, Evangelista M, Sleebs NJ, Rogers K, Pettikiriarachchi A, Kershaw NJ, Eddinger GA, Belair DG, Wilson JL, Eller CH, Raines RT, Murphy WL, Smith BJ, Gellman SH, Fairlie WD J Am Chem Soc. 2015 Aug 28. PMID:26317395<ref>PMID:26317395</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5agw" 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: Checco JW]]
[[Category: F Lee E]]
[[Category: Fairlie WD]]
[[Category: Gellman SH]]
[[Category: Smith BJ]]