{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T00:35:14Z","timestamp":1790728514441,"version":"4.1.0"},"reference-count":44,"publisher":"Wiley","issue":"12","license":[{"start":{"date-parts":[[2019,4,11]],"date-time":"2019-04-11T00:00:00Z","timestamp":1554940800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2019,6]]},"abstract":"\n \n \n Four\n TEAD<\/jats:styled-content>\n transcription factors (\n TEAD<\/jats:styled-content>\n 1\u20134) mediate the signalling output of the Hippo pathway that controls organ size in humans.\n TEAD<\/jats:styled-content>\n transcriptional activity is regulated via interactions with the\n YAP<\/jats:styled-content>\n ,\n TAZ<\/jats:styled-content>\n and\n VGLL<\/jats:styled-content>\n proteins. A mutation in the\n \n TEAD<\/jats:styled-content>\n 1\n <\/jats:italic>\n gene, Tyr421His, has been identified in patients suffering from Sveinsson's chorioretinal atrophy (\n SCA<\/jats:styled-content>\n ), an autosomal dominant eye disease. This mutation prevents the\n YAP<\/jats:styled-content>\n \/\n TAZ<\/jats:styled-content>\n :\n TEAD<\/jats:styled-content>\n 1 interaction. In this study, we measure the affinity of\n YAP<\/jats:styled-content>\n ,\n TAZ<\/jats:styled-content>\n and\n VGLL<\/jats:styled-content>\n 1 for the four human\n TEAD<\/jats:styled-content>\n s and find that they have a similar affinity for all\n TEAD<\/jats:styled-content>\n s. We quantitate the effect of the mutation found in\n SCA<\/jats:styled-content>\n patients and show that it destabilizes the\n YAP<\/jats:styled-content>\n \/\n TAZ<\/jats:styled-content>\n :\n TEAD<\/jats:styled-content>\n interaction by about 3\u00a0kcal\u00b7mol\n \u22121<\/jats:sup>\n . We determine the structure of\n YAP<\/jats:styled-content>\n in complex with this mutant form of\n TEAD<\/jats:styled-content>\n and show that the histidine residue adopts different conformations at the binding interface. The presence of this flexible residue induces the destabilization of several H\u2010bonds and the loss of van der Waals contacts, which explains why the Tyr421His\n \n TEAD<\/jats:sup>\n <\/jats:styled-content>\n 1<\/jats:sup>\n mutation has such a large destabilizing effect on the formation of the\n YAP<\/jats:styled-content>\n :\n TEAD<\/jats:styled-content>\n complex.\n <\/jats:p>\n <\/jats:sec>\n \n Database<\/jats:title>\n \n The crystallographic data have been deposited at the RSCB Protein Data Bank (PDB,\n www.pdb.org<\/jats:ext-link>\n ) with the access codes:\n 6HIL<\/jats:ext-link>\n (wt\n YAP<\/jats:sup>\n :Tyr421His\n TEAD1<\/jats:sup>\n ),\n 6HIK<\/jats:ext-link>\n (wt\n YAP<\/jats:sup>\n :Tyr429His\n TEAD4<\/jats:sup>\n )\n <\/jats:p>\n <\/jats:sec>","DOI":"10.1111\/febs.14817","type":"journal-article","created":{"date-parts":[[2019,3,23]],"date-time":"2019-03-23T10:43:49Z","timestamp":1553337829000},"page":"2381-2398","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":30,"title":["Molecular and structural characterization of a\n TEAD<\/scp>\n mutation at the origin of Sveinsson's chorioretinal atrophy"],"prefix":"10.1111","volume":"286","author":[{"given":"Fedir","family":"Bokhovchuk","sequence":"first","affiliation":[{"name":"Disease Area Oncology Novartis Institutes for Biomedical Research Basel Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yannick","family":"Mesrouze","sequence":"additional","affiliation":[{"name":"Disease Area Oncology Novartis Institutes for Biomedical Research Basel 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