About: Dissection of Binding between a Phosphorylated Tyrosine Hydroxylase Peptide and 14-3-3zéta: A Complex Story Elucidated by NMR

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About: Dissection of Binding between a Phosphorylated Tyrosine Hydroxylase Peptide and 14-3-3zéta: A Complex Story Elucidated by NMR Goto Sponge NotDistinct Permalink

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
rdfs:seeAlso	http://www.sciencedirect.com/science/article/pii/S0006349514010121
Description	Human tyrosine hydroxylase activity is regulated by phosphorylation of its N-terminus and by an interaction with the modulator 14-3-3 proteins. We investigated the binding of singly or doubly phosphorylated and thiophosphorylated peptides, comprising the first 50 amino acids of human tyrosine hydroxylase, isoform 1 (hTH1), that contain the critical interaction domain, to 14-3-3zéta, by 31P NMR. Single phosphorylation at S19 generates a high affinity 14-3-3zéta binding epitope, whereas singly S40-phosphorylated peptide interacts with 14-3-3zéta one order-of-magnitude weaker than the S19-phosphorylated peptide. Human tyrosine hydroxylase activity is regulated by phosphorylation of its N-terminus and by an interaction with the modulator 14-3-3 proteins. We investigated the binding of singly or doubly phosphorylated and thiophosphorylated peptides, comprising the first 50 amino acids of human tyrosine hydroxylase, isoform 1 (hTH1), that contain the critical interaction domain, to 14-3-3zéta, by 31P NMR. Single phosphorylation at S19 generates a high affinity 14-3-3zéta binding epitope, whereas singly S40-phosphorylated peptide interacts with 14-3-3zéta one order-of-magnitude weaker than the S19-phosphorylated peptide. (en)
Title	Dissection of Binding between a Phosphorylated Tyrosine Hydroxylase Peptide and 14-3-3zéta: A Complex Story Elucidated by NMR Dissection of Binding between a Phosphorylated Tyrosine Hydroxylase Peptide and 14-3-3zéta: A Complex Story Elucidated by NMR (en)
skos:prefLabel	Dissection of Binding between a Phosphorylated Tyrosine Hydroxylase Peptide and 14-3-3zéta: A Complex Story Elucidated by NMR Dissection of Binding between a Phosphorylated Tyrosine Hydroxylase Peptide and 14-3-3zéta: A Complex Story Elucidated by NMR (en)
skos:notation	RIV/00216224:14740/14:00077266!RIV15-MSM-14740___
http://linked.open...avai/riv/aktivita	R
http://linked.open...avai/riv/aktivity	R
http://linked.open...iv/cisloPeriodika	9
http://linked.open...vai/riv/dodaniDat	2015
http://linked.open...aciTvurceVysledku	Sklenář, Vladimír Hritz, Jozef
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Masarykova univerzita / Středoevropský technologický institut
http://linked.open...dnocenehoVysledku	11776
http://linked.open...ai/riv/idVysledku	RIV/00216224:14740/14:00077266
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	STRUCTURAL BASIS; PROTEINS; DOMAIN; SITES; GENE (en)
http://linked.open.../riv/klicoveSlovo	DOMAIN GENE SITES STRUCTURAL BASIS PROTEINS
http://linked.open...odStatuVydavatele	US - Spojené státy americké
http://linked.open...ontrolniKodProRIV	[3A4E41834653]
http://linked.open...i/riv/nazevZdroje	Biophysical Journal
http://linked.open...in/vavai/riv/obor	BO
http://linked.open...ichTvurcuVysledku	2 (xsd:int)
http://linked.open...cetTvurcuVysledku	6 (xsd:int)
http://linked.open...UplatneniVysledku	2014
http://linked.open...v/svazekPeriodika	107
http://linked.open...iv/tvurceVysledku	Sklenář, Vladimír Hritz, Jozef Byeon, In-Ja L. Gronenborn, Angela M. Krzysiak, Troyi Martinez, Aurora
http://linked.open...ain/vavai/riv/wos	000344232500020
issn	0006-3495
number of pages	10 (xsd:int)
http://bibframe.org/vocab/doi	10.1016/j.bpj.2014.08.039
http://localhost/t...ganizacniJednotka	14740

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