6mbb

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'''Unreleased structure'''
 
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The entry 6mbb is ON HOLD until Paper Publication
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==Human Bfl-1 in complex with the designed peptide dF1==
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<StructureSection load='6mbb' size='340' side='right' caption='[[6mbb]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6mbb]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MBB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MBB 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=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=6mbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mbb OCA], [http://pdbe.org/6mbb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mbb RCSB], [http://www.ebi.ac.uk/pdbsum/6mbb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mbb ProSAT]</span></td></tr>
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</table>
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== 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).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Understanding the relationship between protein sequence and structure well enough to design new proteins with desired functions is a longstanding goal in protein science. Here, we show that recurring tertiary structural motifs (TERMs) in the PDB provide rich information for protein-peptide interaction prediction and design. TERM statistics can be used to predict peptide binding energies for Bcl-2 family proteins as accurately as widely used structure-based tools. Furthermore, design using TERM energies (dTERMen) rapidly and reliably generates high-affinity peptide binders of anti-apoptotic proteins Bfl-1 and Mcl-1 with just 15%-38% sequence identity to any known native Bcl-2 family protein ligand. High-resolution structures of four designed peptides bound to their targets provide opportunities to analyze the strengths and limitations of the computational design method. Our results support dTERMen as a powerful approach that can complement existing tools for protein engineering.
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Authors:
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Tertiary Structural Motif Sequence Statistics Enable Facile Prediction and Design of Peptides that Bind Anti-apoptotic Bfl-1 and Mcl-1.,Frappier V, Jenson JM, Zhou J, Grigoryan G, Keating AE Structure. 2019 Feb 12. pii: S0969-2126(19)30008-5. doi:, 10.1016/j.str.2019.01.008. PMID:30773399<ref>PMID:30773399</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6mbb" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Jenson, J M]]
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[[Category: Keating, A E]]
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[[Category: Anti-apoptotic bcl-2]]
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[[Category: Apoptosis]]
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[[Category: Design]]
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[[Category: Inhibitor]]

Revision as of 07:33, 6 March 2019

Human Bfl-1 in complex with the designed peptide dF1

6mbb, resolution 1.59Å

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