(1)H, (13)C, (15)N resonance assignment of human YAP 50–171 fragment

Yes associated protein (YAP) is an intrinsically disordered protein that plays a major role in the Hippo pathway, regulating organ size, cell proliferation, apoptosis, and is associated with cancer development. Therefore, the binding between YAP and TEAD is an interesting target for cancer therapy....

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Detalles Bibliográficos
Autores principales: Feichtinger, Michael, Sára, Tomáš, Platzer, Gerald, Mateos, Borja, Bokhovchuk, Fedir, Chène, Patrick, Konrat, Robert
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2018
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5869869/
https://www.ncbi.nlm.nih.gov/pubmed/29372459
http://dx.doi.org/10.1007/s12104-018-9805-8
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author Feichtinger, Michael
Sára, Tomáš
Platzer, Gerald
Mateos, Borja
Bokhovchuk, Fedir
Chène, Patrick
Konrat, Robert
author_facet Feichtinger, Michael
Sára, Tomáš
Platzer, Gerald
Mateos, Borja
Bokhovchuk, Fedir
Chène, Patrick
Konrat, Robert
author_sort Feichtinger, Michael
collection PubMed
description Yes associated protein (YAP) is an intrinsically disordered protein that plays a major role in the Hippo pathway, regulating organ size, cell proliferation, apoptosis, and is associated with cancer development. Therefore, the binding between YAP and TEAD is an interesting target for cancer therapy. The TEAD binding domain of YAP was mapped to protein residues 50–171. To obtain further structural insights into this 12 kDa segment of YAP, we report a backbone and a partial sidechain assignment of recombinant YAP 50–171.
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spelling pubmed-58698692018-03-28 (1)H, (13)C, (15)N resonance assignment of human YAP 50–171 fragment Feichtinger, Michael Sára, Tomáš Platzer, Gerald Mateos, Borja Bokhovchuk, Fedir Chène, Patrick Konrat, Robert Biomol NMR Assign Article Yes associated protein (YAP) is an intrinsically disordered protein that plays a major role in the Hippo pathway, regulating organ size, cell proliferation, apoptosis, and is associated with cancer development. Therefore, the binding between YAP and TEAD is an interesting target for cancer therapy. The TEAD binding domain of YAP was mapped to protein residues 50–171. To obtain further structural insights into this 12 kDa segment of YAP, we report a backbone and a partial sidechain assignment of recombinant YAP 50–171. Springer Netherlands 2018-01-25 2018 /pmc/articles/PMC5869869/ /pubmed/29372459 http://dx.doi.org/10.1007/s12104-018-9805-8 Text en © The Author(s) 2018 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Article
Feichtinger, Michael
Sára, Tomáš
Platzer, Gerald
Mateos, Borja
Bokhovchuk, Fedir
Chène, Patrick
Konrat, Robert
(1)H, (13)C, (15)N resonance assignment of human YAP 50–171 fragment
title (1)H, (13)C, (15)N resonance assignment of human YAP 50–171 fragment
title_full (1)H, (13)C, (15)N resonance assignment of human YAP 50–171 fragment
title_fullStr (1)H, (13)C, (15)N resonance assignment of human YAP 50–171 fragment
title_full_unstemmed (1)H, (13)C, (15)N resonance assignment of human YAP 50–171 fragment
title_short (1)H, (13)C, (15)N resonance assignment of human YAP 50–171 fragment
title_sort (1)h, (13)c, (15)n resonance assignment of human yap 50–171 fragment
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5869869/
https://www.ncbi.nlm.nih.gov/pubmed/29372459
http://dx.doi.org/10.1007/s12104-018-9805-8
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