Related ArticlesCharacterization of the interactions between inhibitor-1 and recombinant PP1 by NMR spectroscopy.
Sci Rep. 2018 Jan 08;8(1):50
Authors: Liang CT, Lin YS, Huang YC, Huang HL, Yang JQ, Wu TH, Chang CF, Huang SJ, Huang HB, Lin TH
Abstract
Inhibitor-1 is converted into a potent inhibitor of native protein phosphatase-1 (PP1) when Thr35 is phosphorylated by cAMP-dependent protein kinase (PKA). However, PKA-phosphorylated form of inhibitor-1 displayed a weak activity in inhibition of recombinant PP1. The mechanism for the impaired activity of PKA-phosphorylated inhibitor-1 toward inhibition of recombinant PP1 remained elusive. By using NMR spectroscopy in combination with site-directed mutagenesis and inhibitory assay, we found that the interaction between recombinant PP1 and the consensus PP1-binding motif of PKA-thiophosphorylated form of inhibitor-1 was unexpectedly weak. Unlike binding to native PP1, the subdomains 1 (residues around and including the phosphorylated Thr35) and 2 (the consensus PP1-binding motif) of PKA-thiophosphorylated form of inhibitor-1 do not exhibit a synergistic effect in inhibition of recombinant PP1. This finding implied that a slight structural discrepancy exists between native and recombinant PP1, resulting in PKA-thiophosphorylated form of inhibitor-1 displaying a different affinity to native and recombinant enzyme.
[NMR paper] Recombinant expression of Ixolaris, a Kunitz-type inhibitor from the tick salivary gland, for NMR studies.
Recombinant expression of Ixolaris, a Kunitz-type inhibitor from the tick salivary gland, for NMR studies.
Related Articles Recombinant expression of Ixolaris, a Kunitz-type inhibitor from the tick salivary gland, for NMR studies.
Protein Expr Purif. 2017 Jul 19;:
Authors: De Paula VS, Silva FHS, Francischetti IMB, Monteiro RQ, Valente AP
Abstract
Ixolaris is an anticoagulant protein identified in the tick saliva of Ixodes scapularis. Ixolaris contains 2 Kunitz like domains and binds to Factor Xa or Factor X as a scaffold for...
nmrlearner
Journal club
0
07-24-2017 10:10 AM
[NMR paper] Characterization of Protein-Carbohydrate Interactions by NMR Spectroscopy.
Characterization of Protein-Carbohydrate Interactions by NMR Spectroscopy.
Related Articles Characterization of Protein-Carbohydrate Interactions by NMR Spectroscopy.
Methods Mol Biol. 2017;1588:143-156
Authors: Grondin JM, Langelaan DN, Smith SP
Abstract
Solution-state nuclear magnetic resonance (NMR) spectroscopy can be used to monitor protein-carbohydrate interactions. Two-dimensional (1)H-(15)N heteronuclear single quantum coherence (HSQC)-based techniques described in this chapter can be used quickly and effectively to...
nmrlearner
Journal club
0
04-19-2017 01:07 PM
[NMR paper] Purification and Characterization of Recombinant N-Terminally Pyroglutamate-Modified Amyloid-? Variants and Structural Analysis by Solution NMR Spectroscopy.
Purification and Characterization of Recombinant N-Terminally Pyroglutamate-Modified Amyloid-? Variants and Structural Analysis by Solution NMR Spectroscopy.
Related Articles Purification and Characterization of Recombinant N-Terminally Pyroglutamate-Modified Amyloid-? Variants and Structural Analysis by Solution NMR Spectroscopy.
PLoS One. 2015;10(10):e0139710
Authors: Dammers C, Gremer L, Neudecker P, Demuth HU, Schwarten M, Willbold D
Abstract
Alzheimer's disease (AD) is the leading cause of dementia in the elderly and is...
NMR structure and dynamics of recombinant wild type and mutated jerdostatin, a selective inhibitor of integrin ?(1) ?(1).
NMR structure and dynamics of recombinant wild type and mutated jerdostatin, a selective inhibitor of integrin ?(1) ?(1).
NMR structure and dynamics of recombinant wild type and mutated jerdostatin, a selective inhibitor of integrin ?(1) ?(1).
Proteins. 2011 May 10;
Authors: Carbajo RJ, Sanz L, Mosulén S, Pérez A, Marcinkiewicz C, Pineda-Lucena A, Calvete JJ
NMR analysis of four recombinant jerdostatin molecules was assessed to define the structural basis of two naturally occurring gain-of-function events: C-terminal dipeptide processing and...
nmrlearner
Journal club
0
06-10-2011 11:52 AM
[NMR paper] Recombinant locust apolipophorin III: characterization and NMR spectroscopy.
Recombinant locust apolipophorin III: characterization and NMR spectroscopy.
Related Articles Recombinant locust apolipophorin III: characterization and NMR spectroscopy.
Biochim Biophys Acta. 1998 Jul 31;1393(1):99-107
Authors: Weers PM, Wang J, Van der Horst DJ, Kay CM, Sykes BD, Ryan RO
Apolipophorin III (apoLp-III) from the locust Locusta migratoria is an exchangeable apolipoprotein that reversibly binds to lipoproteins. During lipid binding the protein has been proposed to undergo a major conformational change. To study the mechanism of...
nmrlearner
Journal club
0
11-17-2010 11:15 PM
[NMR paper] NMR structural characterization of the CDK inhibitor p19INK4d.
NMR structural characterization of the CDK inhibitor p19INK4d.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR structural characterization of the CDK inhibitor p19INK4d.
FEBS Lett. 1997 Jan 20;401(2-3):127-32
Authors: Kalus W, Baumgartner R, Renner C, Noegel A, Chan FK, Winoto A, Holak TA
p19INK4d is a 165 amino acid protein that belongs to the INK4 family of CDK4 and CDK6 inhibitors. Assignments of 1H, 15N and 13C resonances have enabled the determination of the...
Characterization of the interactions between inhibitor-1 and recombinant PP1 by NMR spectroscopy.
Linear Mode
