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3fdl

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{{Seed}}
 
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[[Image:3fdl.png|left|200px]]
 
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<!--
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==Bim BH3 peptide in complex with Bcl-xL==
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The line below this paragraph, containing "STRUCTURE_3fdl", creates the "Structure Box" on the page.
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<StructureSection load='3fdl' size='340' side='right'caption='[[3fdl]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3fdl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FDL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FDL FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.78&#8491;</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=3fdl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fdl OCA], [https://pdbe.org/3fdl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fdl RCSB], [https://www.ebi.ac.uk/pdbsum/3fdl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fdl ProSAT]</span></td></tr>
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{{STRUCTURE_3fdl| PDB=3fdl | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/B2CL1_HUMAN B2CL1_HUMAN] Potent inhibitor of cell death. Inhibits activation of caspases (By similarity). Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis.<ref>PMID:19917720</ref> <ref>PMID:21840391</ref> Isoform Bcl-X(S) promotes apoptosis.<ref>PMID:19917720</ref> <ref>PMID:21840391</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fd/3fdl_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3fdl ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Get into the groove: The first high-resolution structure of a foldamer bound to a protein target is described (see picture; foldamer in sticks). The foldamer consists of alpha- and beta-amino acid residues and is bound to the anti-apoptotic protein Bcl-x(L). The overall binding mode and key interactions observed in the foldamer/Bcl-x(L) complex mimic those seen in complexes of Bcl-x(L) with natural alpha-peptide ligands. Additional contacts in the foldamer/Bcl-x(L) complex involving beta-amino acid residues appear to contribute to binding affinity.
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===Bim BH3 peptide in complex with Bcl-xL===
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High-Resolution Structural Characterization of a Helical alpha/beta-Peptide Foldamer Bound to the Anti-Apoptotic Protein Bcl-x(L).,Lee EF, Sadowsky JD, Smith BJ, Czabotar PE, Peterson-Kaufman KJ, Colman PM, Gellman SH, Fairlie WD Angew Chem Int Ed Engl. 2009 Feb 19;48(24):4318-4322. PMID:19229915<ref>PMID:19229915</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 3fdl" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19229915}}, adds the Publication Abstract to the page
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*[[B-cell lymphoma proteins 3D structures|B-cell lymphoma proteins 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19229915 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19229915}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3FDL is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FDL OCA].
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==Reference==
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<ref group="xtra">PMID:19229915</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Colman, P M.]]
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[[Category: Large Structures]]
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[[Category: Czabotar, P E.]]
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[[Category: Synthetic construct]]
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[[Category: Fairlie, W D.]]
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[[Category: Colman PM]]
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[[Category: Lee, E F.]]
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[[Category: Czabotar PE]]
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[[Category: Smith, B J.]]
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[[Category: Fairlie WD]]
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[[Category: Alternative splicing]]
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[[Category: Lee EF]]
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[[Category: Apoptosis]]
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[[Category: Smith BJ]]
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[[Category: Helical bundle]]
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[[Category: Membrane]]
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[[Category: Mitochondrion]]
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[[Category: Nucleus]]
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[[Category: Peptide-protein complex]]
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[[Category: Phosphoprotein]]
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[[Category: Transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 10 18:54:18 2009''
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Current revision

Bim BH3 peptide in complex with Bcl-xL

PDB ID 3fdl

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