Dissection of Binding between a Phosphorylated Tyrosine Hydroxylase Peptide and 14-3-3?: A Complex Story Elucidated by NMR.
Biophys J. 2014 Nov 4;107(9):2185-94
Authors: Hritz J, Byeon IJ, Krzysiak T, Martinez A, Sklenar V, Gronenborn AM
Abstract
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 14-3-3?, by (31)P NMR. Single phosphorylation at S19 generates a high affinity 14-3-3? binding epitope, whereas singly S40-phosphorylated peptide interacts with 14-3-3? one order-of-magnitude weaker than the S19-phosphorylated peptide. Analysis of the binding data revealed that the 14-3-3? dimer and the S19- and S40-doubly phosphorylated peptide interact in multiple ways, with three major complexes formed: 1), a single peptide bound to a 14-3-3? dimer via the S19 phosphate with the S40 phosphate occupying the other binding site; 2), a single peptide bound to a 14-3-3? dimer via the S19 phosphorous with the S40 free in solution; or 3), a 14-3-3? dimer with two peptides bound via the S19 phosphorous to each binding site. Our system and data provide information as to the possible mechanisms by which 14-3-3 can engage binding partners that possess two phosphorylation sites on flexible tails. Whether these will be realized in any particular interacting pair will naturally depend on the details of each system.
[NMR paper] Structural characterization by NMR of a double phosphorylated chimeric Peptide vaccine for treatment of Alzheimer's disease.
Structural characterization by NMR of a double phosphorylated chimeric Peptide vaccine for treatment of Alzheimer's disease.
Structural characterization by NMR of a double phosphorylated chimeric Peptide vaccine for treatment of Alzheimer's disease.
Molecules. 2013;18(5):4929-41
Authors: Ramírez-Gualito K, Richter M, Matzapetakis M, Singer D, Berger S
Abstract
Rational design of peptide vaccines becomes important for the treatment of some diseases such as Alzheimer's disease (AD) and related disorders. In this study, as part of a larger...
[NMR paper] NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+
NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump.
Related Articles NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump.
Biochemistry. 1999 Sep 21;38(38):12320-32
Authors: Elshorst B, Hennig M, Försterling H, Diener A, Maurer M, Schulte P, Schwalbe H, Griesinger C, Krebs J, Schmid H, Vorherr T, Carafoli E
The three-dimensional structure of the complex between calmodulin (CaM) and a peptide corresponding to the N-terminal portion of the CaM-binding domain of the...
nmrlearner
Journal club
0
11-18-2010 08:31 PM
[NMR paper] NMR studies of the RRsrc peptide, a tyrosine kinase substrate.
NMR studies of the RRsrc peptide, a tyrosine kinase substrate.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.nrc-cnrc.gc.ca-cisti-journals-rp-gifs-PubMed_logo_e.gif Related Articles NMR studies of the RRsrc peptide, a tyrosine kinase substrate.
Biochem Cell Biol. 1997;75(2):163-9
Authors: Brockbank RL, Vogel HJ
The proton and carbon-13 NMR resonances for the 13-residue synthetic RRsrc peptide were completely assigned using two-dimensional NMR spectroscopy. This peptide contains a tyrosine in position 9 that can be phosphorylated...
nmrlearner
Journal club
0
08-22-2010 03:31 PM
[NMR paper] NMR studies of the RRsrc peptide, a tyrosine kinase substrate.
NMR studies of the RRsrc peptide, a tyrosine kinase substrate.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.nrc-cnrc.gc.ca-cisti-journals-rp-gifs-PubMed_logo_e.gif Related Articles NMR studies of the RRsrc peptide, a tyrosine kinase substrate.
Biochem Cell Biol. 1997;75(2):163-9
Authors: Brockbank RL, Vogel HJ
The proton and carbon-13 NMR resonances for the 13-residue synthetic RRsrc peptide were completely assigned using two-dimensional NMR spectroscopy. This peptide contains a tyrosine in position 9 that can be phosphorylated...
nmrlearner
Journal club
0
08-22-2010 03:03 PM
[NMR paper] Dissection of the basic subdomain of the c-Jun oncoprotein: a structural analysis of
Dissection of the basic subdomain of the c-Jun oncoprotein: a structural analysis of two peptide fragments by CD, Fourier-transform infrared and NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Dissection of the basic subdomain of the c-Jun oncoprotein: a structural analysis of two peptide fragments by CD, Fourier-transform infrared and NMR.
Eur J Biochem. 1996 Feb 1;235(3):699-712
Authors: Krebs D, Dahmani B, Monnot M, Mauffret O,...
nmrlearner
Journal club
0
08-22-2010 02:27 PM
[NMR paper] Tubulin-tyrosine ligase catalyzes covalent binding of 3-fluoro-tyrosine to tubulin: k
Tubulin-tyrosine ligase catalyzes covalent binding of 3-fluoro-tyrosine to tubulin: kinetic and NMR studies.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Tubulin-tyrosine ligase catalyzes covalent binding of 3-fluoro-tyrosine to tubulin: kinetic and NMR studies.
FEBS Lett. 1995 Oct 30;374(2):165-8
Authors: Monasterio O, Nova E, López-Brauet A, Lagos R
The use of 3-fluoro-tyrosine as an alternative substrate for the enzyme tubulin:tyrosine ligase which catalyzes the...