RH421 binds into the ATP-binding site on the Na+/K+-ATPase
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چکیده
منابع مشابه
Cryopyrin/NALP3 binds ATP/dATP, is an ATPase, and requires ATP binding to mediate inflammatory signaling.
The CATERPILLER (CLR/NLR) gene family encodes a family of putative nucleotide-binding proteins important for host defense. Although nucleotide binding is thought to be central to this family, this aspect is largely unstudied. The CATERPILLER protein cryopyrin/NALP3 regulates IL-1beta processing by assembling the multimeric inflammasome complex. Mutations within the exon encoding the nucleotide-...
متن کاملATP-binding is stabilized by a stacking interaction within the binding site of Na+/K+ -ATPase.
Site-directed mutagenesis was applied to modify phenylalanines (Phe(475)Trp, Phe(548)Tyr, and both) to generate mutants on the basis of molecular modeling of the ATP-binding domain of Na(+)/K(+)-ATPase, in order to characterize the forces that stabilize ATP in its binding pocket. Each of the mutants was examined by Raman difference spectroscopy, i.e., as a difference between the spectrum of the...
متن کاملsurvey on the rule of the due & hindering relying on the sheikh ansaris ideas
قاعده مقتضی و مانع در متون فقهی کم و بیش مستند احکام قرار گرفته و مورد مناقشه فقهاء و اصولیین می باشد و مشهور معتقند مقتضی و مانع، قاعده نیست بلکه یکی از مسائل ذیل استصحاب است لذا نگارنده بر آن شد تا پیرامون این قاعده پژوهش جامعی انجام دهد. به عقیده ما مقتضی دارای حیثیت مستقلی است و هر گاه می گوییم مقتضی احراز شد یعنی با ماهیت مستقل خودش محرز گشته و قطعا اقتضاء خود را خواهد داشت مانند نکاح که ...
15 صفحه اولComparative studies on the ATPase-binding sites in Ca2+-ATPase and (Na+ + K+)-ATPase by the use of ATP-analogues.
The effects of ATP-analogues on Ca2+-ATPase and (Na++ K+)-ATPase have been studied. The participation of sulfhydryl groups in the recognition of ATP by both transport ATPases is indicated by the fact, that the disulfide of thioinosine triphosphate inactivates both enzymes. The reactivity of rapidly and slowly reacting sulfhydryl groups in the ATP binding sites of both enzymes is altered by the ...
متن کاملATP binding equilibria of the Na(+),K(+)-ATPase.
Reported values of the dissociation constant, K(d), of ATP with the E1 conformation of the Na(+),K(+)-ATPase fall in two distinct ranges depending on how it is measured. Equilibrium binding studies yield values of 0.1-0.6 microM, whereas presteady-state kinetic studies yield values of 3-14 microM. It is unacceptable that K(d) varies with the experimental method of its determination. Using simul...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Biomembranes
سال: 2017
ISSN: 0005-2736
DOI: 10.1016/j.bbamem.2017.07.016