Backbone and side chain NMR assignment of the heme-nitric oxide/oxygen binding (H-NOX) domain from Nostoc punctiformeBiomolecular NMR Assignments - Tập 16 - Trang 379-384 - 2022
Styliani A. Chasapi, Aikaterini I. Argyriou, Georgios A. Spyroulias
Soluble guanylate cyclase (sGC) is considered as the primary NO receptor across several known eukaryotes. The main interest regarding the biological role and its function, focuses on the H-NOX domain of the β1 subunit. This domain in its active form bears a ferrous b type heme as prosthetic group, which facilitates the binding of NO and other diatomic gases. The key point that still needs to be an...... hiện toàn bộ
Resonance assignments and secondary structure of apolipoprotein E C-terminal domain in DHPC micellesBiomolecular NMR Assignments - Tập 9 - Trang 187-190 - 2014
Chi-Jen Lo, Chia-Lin Chyan, Yi-Chen Chen, Chi-Fon Chang, Hsien-bin Huang, Ta-Hsien Lin
Human apolipoprotein E (apoE) has been known to play a key role in the transport of plasma cholesterol and lipoprotein metabolism. It is an apolipoprotein of 299 amino acids with a molecular mass, ~34 kDa. ApoE has three major isoforms, apoE2, apoE3, and apoE4 which differ only at residue 112 or 158. ApoE consists of two independently folded domains (N-terminal and C-terminal domain) separated by ...... hiện toàn bộ
Backbone chemical shift assignment of a glutamate receptor ligand binding domain in complexes with five partial agonistsBiomolecular NMR Assignments - Tập 1 - Trang 241-243 - 2007
Michael K. Fenwick, Robert E. Oswald
Backbone 1H, 13C, and 15N chemical shifts are reported for complexes of a perdeuterated glutamate receptor ligand binding domain with kainate, willardiine, and 5-substituted fluoro-, bromo-, and iodowillardiine. These ligands are partial agonists that induce distinct current responses at post-synaptic neurons. The chemical shifts pave the way for numerous NMR studies to identify structural and dyn...... hiện toàn bộ
Backbone assignments of the apo and Zn(II) protoporphyrin IX-bound states of the soluble form of rat heme oxygenase-1Biomolecular NMR Assignments - Tập 9 - Trang 197-200 - 2014
Erisa Harada, Masakazu Sugishima, Jiro Harada, Masato Noguchi, Keiichi Fukuyama, Kenji Sugase
In nature, heme is a prosthetic group that is universally used as a cofactor for heme proteins. It is necessary for the execution of fundamental biological processes including electron transfer, oxidation and metabolism. However, free heme is toxic to cells, because of its capability to enhance oxidative stress, hence its cellular concentration is strictly regulated through multiple mechanisms. He...... hiện toàn bộ
Resonance assignments of the 56 kDa chimeric avidin in the biotin-bound and free formsBiomolecular NMR Assignments - Tập 7 - Trang 35-38 - 2012
Helena Tossavainen, Satu H. Helppolainen, Juha A. E. Määttä, Tero Pihlajamaa, Vesa P. Hytönen, Markku S. Kulomaa, Perttu Permi
Avidin is a homotetrameric ~56 kDa protein found in chicken egg white. Avidin’s ability to bind biotin with a very high affinity has widely been exploited in biotechnological applications. Protein engineering has further diversified avidin’s feasibility. ChiAVD(I117Y) is a product of rational protein engineering. It is a hyperthermostable synthetic hybrid of avidin and avidin-related protein 4 (AV...... hiện toàn bộ
1H, 15N, 13C backbone resonance assignments of human soluble catechol O-methyltransferase in complex with S-adenosyl-l-methionine and 3,5-dinitrocatecholBiomolecular NMR Assignments - Tập 11 - Trang 57-61 - 2016
Sylwia Czarnota, Nicola J. Baxter, Matthew J. Cliff, Jonathan P. Waltho, Nigel S. Scrutton, Sam Hay
Catechol O-methyltransferase (COMT) is an enzyme that plays a major role in catechol neurotransmitter deactivation. Inhibition of COMT can increase neurotransmitter levels, which provides a means of treatment for Parkinson’s disease, schizophrenia and depression. COMT exists as two isozymes: a soluble cytoplasmic form (S-COMT), expressed in the liver and kidneys and a membrane-bound form (MB-COMT)...... hiện toàn bộ