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| Description
| - he structural stability of the large cytoplasmic domain (H-4-H-5 loop) of mouse alpha(1) subunit of Na+/K+ ATPase (L354-I777), the number and the location of its binding sites for 2'-3'-O-(trinitrophenyl) adenosine 5'-triphosphate (TNP-ATP) and p-nitrophenylphosphate (pNPP) were investigated. C- and N-terminal shortening revealed that neither part of the phosphorylation (P)-domain are necessary for TNP-ATP binding. There is no indication of a second ATP site on the P-domain of the isolated loop, even though others reported previously of its existence by TNP-N(3)ADP affinity labeling of the full enzyme. Fluorescein isothiocyanate (FITC)-anisotropy measurements reveal a considerable stability of the nucleotide (N)-domain suggesting that it may not undergo a substantial conformational change upon ATP binding. The FITC modified loop showed only slightly diminished phosphatase activity, most likely due to a pNPP site on the N-domain around N398 whose mutation to D reduced the phosphatase...
- he structural stability of the large cytoplasmic domain (H-4-H-5 loop) of mouse alpha(1) subunit of Na+/K+ ATPase (L354-I777), the number and the location of its binding sites for 2'-3'-O-(trinitrophenyl) adenosine 5'-triphosphate (TNP-ATP) and p-nitrophenylphosphate (pNPP) were investigated. C- and N-terminal shortening revealed that neither part of the phosphorylation (P)-domain are necessary for TNP-ATP binding. There is no indication of a second ATP site on the P-domain of the isolated loop, even though others reported previously of its existence by TNP-N(3)ADP affinity labeling of the full enzyme. Fluorescein isothiocyanate (FITC)-anisotropy measurements reveal a considerable stability of the nucleotide (N)-domain suggesting that it may not undergo a substantial conformational change upon ATP binding. The FITC modified loop showed only slightly diminished phosphatase activity, most likely due to a pNPP site on the N-domain around N398 whose mutation to D reduced the phosphatase... (en)
- Zkoumali jsme strukturní stabilitu velké cytoplasmatické domény (H4-H5 klička) z myší ?1 podjednotky Na+/K+ ATPázy (L354-I777), počet a umístění vazebných míst pro 2´-3´-O-(trinitrofenyl) adenosin 5´-trifosfát (TNP-ATP) a p-nitrofenylfosfát (pNPP). Zkrácení C- a N- konce ukazuje, že žádná z částí fosforilační (P)-domény není nezbytná pro vázání TNP-ATP. Nemáme žádné náznaky o druhém vazebním místě ATP na P-doméně isolované kličky, přestože jiní dříva psali o jeho existenci pomocí TNP-N3ADP afinitním značením celého enzymu. Fluorescein isothiocyanate (FITC)-anizotropní měření ukázala značnou stabilitu nukleotidové (N)-domény, což naznačuje, že tato doména neprochází podstatnými konformačními změnami při vázání ATP. FITCem modifikovaná klička ukázala pouze slabě zmenšenou fosfatázovou aktivitu, s největší pravděpodobností kvůli pNPP vazebnímu místu na N-doméně kolem N398, jehož mutace na D snížily fosfatázovou aktivitu o 50 %. Aminokyseliny vytvářející toto vazebné místo pro pNPP (M38... (cs)
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| Title
| - The phosphatase activity of the isolated H4-H5 loop of Na+/K+ ATPase resides outside its ATP binding site
- Fosfatázová aktivita isolované H4-H5 kličky z Na+/K+ ATPázy se nachází mimo vazebné místo pro ATP (cs)
- The phosphatase activity of the isolated H4-H5 loop of Na+/K+ ATPase resides outside its ATP binding site (en)
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| skos:prefLabel
| - The phosphatase activity of the isolated H4-H5 loop of Na+/K+ ATPase resides outside its ATP binding site
- Fosfatázová aktivita isolované H4-H5 kličky z Na+/K+ ATPázy se nachází mimo vazebné místo pro ATP (cs)
- The phosphatase activity of the isolated H4-H5 loop of Na+/K+ ATPase resides outside its ATP binding site (en)
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| skos:notation
| - RIV/67179843:_____/04:00031718!RIV06-AV0-67179843
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| http://linked.open.../vavai/riv/strany
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| http://linked.open...avai/riv/aktivita
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| http://linked.open...avai/riv/aktivity
| - P(GA204/01/0254), P(GA204/01/1001), P(GA309/02/1479), P(GP206/03/D082), P(LN00A141), Z(AV0Z5011922)
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| http://linked.open...iv/cisloPeriodika
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| http://linked.open...vai/riv/dodaniDat
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| http://linked.open...aciTvurceVysledku
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| http://linked.open.../riv/druhVysledku
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| http://linked.open...iv/duvernostUdaju
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| http://linked.open...titaPredkladatele
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| http://linked.open...dnocenehoVysledku
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| http://linked.open...ai/riv/idVysledku
| - RIV/67179843:_____/04:00031718
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| http://linked.open...riv/jazykVysledku
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| http://linked.open.../riv/klicovaSlova
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| http://linked.open.../riv/klicoveSlovo
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| http://linked.open...odStatuVydavatele
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| http://linked.open...ontrolniKodProRIV
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| http://linked.open...i/riv/nazevZdroje
| - European Journal of Biochemistry
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| http://linked.open...in/vavai/riv/obor
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| http://linked.open...ichTvurcuVysledku
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| http://linked.open...cetTvurcuVysledku
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| http://linked.open...vavai/riv/projekt
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| http://linked.open...UplatneniVysledku
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| http://linked.open...v/svazekPeriodika
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| http://linked.open...iv/tvurceVysledku
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| http://linked.open...n/vavai/riv/zamer
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| issn
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| number of pages
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