6gei | pdb_00006gei

TEAD4 (216-434);E263A+Y429F COMPLEXED WITH YAP PEPTIDE (60- 100);S94A AND MYRISTOATE (COVALENTLY BOUND TO LYS344, NOT CYS367!) AT 1.65A (P41212 CRYSTAL FORM); MYRISTOYLATION WAS DONE BY ADDING MYR-COA

spinqualitylabelsall models 6gei, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6gei is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.65Å Ligands: ACE, MYR, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 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. Publication Abstract from PubMed Many interactions between proteins are mediated by intrinsically disordered regions (IDRs). Intrinsically disordered proteins (IDPs) do not adopt a stable three-dimensional structure in their unbound form, but they become more structured upon binding to their partners. In this communication, we study how a bound IDR adapts to mutations, preventing the formation of hydrogen bonds at the binding interface that need a precise positioning of the interacting residues to be formed. We use as model the YAP:TEAD interface, where one YAP (IDP) and two TEAD residues form hydrogen bonds via their side chain. Our study shows that the conformational flexibility of bound YAP and the reorganization of water molecules at the interface help to reduce the energetic constraints created by the loss of H-bonds at the interface. The residual flexibility/dynamic of bound IDRs and water might therefore be key for the adaptation of IDPs to different interface landscapes and to mutations occurring at binding interfaces. This article is protected by copyright. All rights reserved. Adaptation of the bound intrinsically disordered protein YAP to mutations at the YAP:TEAD interface.,Mesrouze Y, Bokhovchuk F, Izaac A, Meyerhofer M, Zimmermann C, Fontana P, Schmelzle T, Erdmann D, Furet P, Kallen J, Chene P Protein Sci. 2018 Jul 29. doi: 10.1002/pro.3493. PMID:30058229 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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