About: Phe475 and Glu446 but not Ser445 participate in ATP-binding to the alfa-subunit of NA/K-ATPase

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About: Phe475 and Glu446 but not Ser445 participate in ATP-binding to the alfa-subunit of NA/K-ATPase Goto Sponge NotDistinct Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	The ATP-binding site of Na+/K+-ATPase is localized on the large cytoplasmic loop of the small alpha, Greek-subunit between transmembrane helices H4 and H5. Site-directed mutagenesis was performed to identify residues involved in ATP binding. On the basis of our recently developed model of this loop, Ser445, Glu446, and Phe475 were proposed to be close to the binding pocket. Replacement of Phe475 with Trp and Glu446 with Gln profoundly reduced the binding of ATP, whereas the substitution of Ser445 with Ala did not affect ATP binding. Fluorescence measurements of the fluorescent analog TNP-ATP, however, indicated that Ser445 is close to the binding site, although it does not participate in binding The ATP-binding site of Na+/K+-ATPase is localized on the large cytoplasmic loop of the small alpha, Greek-subunit between transmembrane helices H4 and H5. Site-directed mutagenesis was performed to identify residues involved in ATP binding. On the basis of our recently developed model of this loop, Ser445, Glu446, and Phe475 were proposed to be close to the binding pocket. Replacement of Phe475 with Trp and Glu446 with Gln profoundly reduced the binding of ATP, whereas the substitution of Ser445 with Ala did not affect ATP binding. Fluorescence measurements of the fluorescent analog TNP-ATP, however, indicated that Ser445 is close to the binding site, although it does not participate in binding (en)
Title	Phe475 and Glu446 but not Ser445 participate in ATP-binding to the alfa-subunit of NA/K-ATPase Phe475 and Glu446 but not Ser445 participate in ATP-binding to the alfa-subunit of NA/K-ATPase (en)
skos:prefLabel	Phe475 and Glu446 but not Ser445 participate in ATP-binding to the alfa-subunit of NA/K-ATPase Phe475 and Glu446 but not Ser445 participate in ATP-binding to the alfa-subunit of NA/K-ATPase (en)
skos:notation	RIV/00216208:11310/02:00007337!RIV/2003/MSM/113103/N
http://linked.open.../vavai/riv/strany	154;159
http://linked.open...avai/riv/aktivita	P Z
http://linked.open...avai/riv/aktivity	P(LN00A026), Z(MSM 113100003)
http://linked.open...iv/cisloPeriodika	1
http://linked.open...vai/riv/dodaniDat	2003
http://linked.open...aciTvurceVysledku	Hofbauerová, Kateřina
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	Univerzita Karlova v Praze / Přírodovědecká fakulta
http://linked.open...dnocenehoVysledku	658161
http://linked.open...ai/riv/idVysledku	RIV/00216208:11310/02:00007337
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	NA/K-ATPase; Fluorescence spectroskopy; ATP-binding site; TNP-ATP (en)
http://linked.open.../riv/klicoveSlovo	ATP-binding site Fluorescence spectroskopy NA/K-ATPase TNP-ATP
http://linked.open...odStatuVydavatele	US - Spojené státy americké
http://linked.open...ontrolniKodProRIV	[9DA53475F350]
http://linked.open...i/riv/nazevZdroje	Biochemical and Biophysical Research Communications
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	1 (xsd:int)
http://linked.open...cetTvurcuVysledku	5 (xsd:int)
http://linked.open...ocetUcastnikuAkce	0 (xsd:int)
http://linked.open...nichUcastnikuAkce	0 (xsd:int)
http://linked.open...vavai/riv/projekt	Center of molecular and cellular immunology
http://linked.open...UplatneniVysledku	2002
http://linked.open...v/svazekPeriodika	297
http://linked.open...iv/tvurceVysledku	Hofbauerová, Kateřina
http://linked.open...n/vavai/riv/zamer	http://linked.opendata.cz/resource/domain/vavai/zamer/MSM%20113100003
issn	0006-291X
number of pages	6 (xsd:int)
http://localhost/t...ganizacniJednotka	11310

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