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6q36

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'''Unreleased structure'''
 
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The entry 6q36 is ON HOLD until Paper Publication
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==TEAD4(216-434) complexed with optimized peptide 9 and myristoate (covalently bound) at 2.01A resolution: Structure-based design of potent linear peptide inhibitors of the YAP-TEAD protein-protein interaction derived from the YAP omega-loop sequence==
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<StructureSection load='6q36' size='340' side='right'caption='[[6q36]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6q36]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q36 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6Q36 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=2JH:3-CYCLOBUTYL-L-ALANINE'>2JH</scene>, <scene name='pdbligand=6CW:6-CHLORO-L-TRYPTOPHAN'>6CW</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=ALN:NAPHTHALEN-2-YL-3-ALANINE'>ALN</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</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=6q36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q36 OCA], [http://pdbe.org/6q36 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6q36 RCSB], [http://www.ebi.ac.uk/pdbsum/6q36 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6q36 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/TEAD4_HUMAN TEAD4_HUMAN]] Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction. Binds specifically and non-cooperatively to the Sph and GT-IIC 'enhansons' (5'-GTGGAATGT-3') and activates transcription. Binds to the M-CAT motif.<ref>PMID:18579750</ref> <ref>PMID:19324877</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The YAP-TEAD protein-protein interaction is a potential therapeutic target to treat cancers in which the Hippo signaling pathway is deregulated. However, the extremely large surface of interaction between the two proteins presents a formidable challenge for a small molecule interaction disrupter approach. We have accomplished progress towards showing the feasibility of this approach by the identification of a 15-mer peptide able to potently (nanomolar range) disrupt the YAP-TEAD interaction by targeting only one of the two important sites of interaction. This peptide, incorporating non-natural amino acids selected by structure-based design, is derived from the Omega-loop sequence 85-99 of YAP.
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Authors: Kallen, J.
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Structure-based design of potent linear peptide inhibitors of the YAP-TEAD protein-protein interaction derived from the YAP omega-loop sequence.,Furet P, Salem B, Mesrouze Y, Schmelzle T, Lewis I, Kallen J, Chene P Bioorg Med Chem Lett. 2019 Jun 18. pii: S0960-894X(19)30402-0. doi:, 10.1016/j.bmcl.2019.06.022. PMID:31235263<ref>PMID:31235263</ref>
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Description: TEAD4(216-434) complexed with optimized peptide 9 and myristoate (covalently bound) at 2.01A resolution: Structure-based design of potent linear peptide inhibitors of the YAP-TEAD protein-protein interaction derived from the YAP omega-loop sequence
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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 6q36" 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: Large Structures]]
[[Category: Kallen, J]]
[[Category: Kallen, J]]
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[[Category: Co-activator]]
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[[Category: Transcription]]
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[[Category: Transcription factor]]
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[[Category: Transcription regulation]]

Revision as of 06:00, 3 July 2019

TEAD4(216-434) complexed with optimized peptide 9 and myristoate (covalently bound) at 2.01A resolution: Structure-based design of potent linear peptide inhibitors of the YAP-TEAD protein-protein interaction derived from the YAP omega-loop sequence

PDB ID 6q36

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