The structures of the kinase domain and UBA domain of MPK38 suggest the activation mechanism for kinase activity

The structure of a crystal of MPK38 (T167E), which consists of a kinase domain and a UBA domain, in complex with AMP-PNP is reported at 2.4 Å resolution. The structure indicates that the activation of MPK38 is induced by the UBA linker restraining the motion of the αC helix and by phosphorylation of...

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Main Authors:	Cho, Yong-Soon, Yoo, Jiho, Park, Soomin, Cho, Hyun-Soo
Format:	Online
Language:	English
Published:	International Union of Crystallography 2014
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3940201/

id	pubmed-3940201
recordtype	oai_dc
spelling	pubmed-39402012014-03-04 The structures of the kinase domain and UBA domain of MPK38 suggest the activation mechanism for kinase activity Cho, Yong-Soon Yoo, Jiho Park, Soomin Cho, Hyun-Soo Research Papers The structure of a crystal of MPK38 (T167E), which consists of a kinase domain and a UBA domain, in complex with AMP-PNP is reported at 2.4 Å resolution. The structure indicates that the activation of MPK38 is induced by the UBA linker restraining the motion of the αC helix and by phosphorylation of Thr167 stabilizing the activation loop. International Union of Crystallography 2014-01-31 /pmc/articles/PMC3940201/ /pubmed/24531485 http://dx.doi.org/10.1107/S1399004713027806 Text en © Cho et al. 2014 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Cho, Yong-Soon Yoo, Jiho Park, Soomin Cho, Hyun-Soo
spellingShingle	Cho, Yong-Soon Yoo, Jiho Park, Soomin Cho, Hyun-Soo The structures of the kinase domain and UBA domain of MPK38 suggest the activation mechanism for kinase activity
author_facet	Cho, Yong-Soon Yoo, Jiho Park, Soomin Cho, Hyun-Soo
author_sort	Cho, Yong-Soon
title	The structures of the kinase domain and UBA domain of MPK38 suggest the activation mechanism for kinase activity
title_short	The structures of the kinase domain and UBA domain of MPK38 suggest the activation mechanism for kinase activity
title_full	The structures of the kinase domain and UBA domain of MPK38 suggest the activation mechanism for kinase activity
title_fullStr	The structures of the kinase domain and UBA domain of MPK38 suggest the activation mechanism for kinase activity
title_full_unstemmed	The structures of the kinase domain and UBA domain of MPK38 suggest the activation mechanism for kinase activity
title_sort	structures of the kinase domain and uba domain of mpk38 suggest the activation mechanism for kinase activity
description	The structure of a crystal of MPK38 (T167E), which consists of a kinase domain and a UBA domain, in complex with AMP-PNP is reported at 2.4 Å resolution. The structure indicates that the activation of MPK38 is induced by the UBA linker restraining the motion of the αC helix and by phosphorylation of Thr167 stabilizing the activation loop.
publisher	International Union of Crystallography
publishDate	2014
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3940201/
_version_	1612063558075416576

The structures of the kinase domain and UBA domain of MPK38 suggest the activation mechanism for kinase activity

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