. . "1"^^ . . . . . . . . "NL - Nizozemsko" . "19" . "RIV/67179843:_____/04:00031718!RIV06-AV0-67179843" . . "[4E86A113DF9E]" . "The phosphatase activity of the isolated H4-H5 loop of Na+/K+ ATPase resides outside its ATP binding site" . . "Zkoumali jsme strukturn\u00ED stabilitu velk\u00E9 cytoplasmatick\u00E9 dom\u00E9ny (H4-H5 kli\u010Dka) z my\u0161\u00ED ?1 podjednotky Na+/K+ ATP\u00E1zy (L354-I777), po\u010Det a um\u00EDst\u011Bn\u00ED vazebn\u00FDch m\u00EDst pro 2\u00B4-3\u00B4-O-(trinitrofenyl) adenosin 5\u00B4-trifosf\u00E1t (TNP-ATP) a p-nitrofenylfosf\u00E1t (pNPP). Zkr\u00E1cen\u00ED C- a N- konce ukazuje, \u017Ee \u017E\u00E1dn\u00E1 z \u010D\u00E1st\u00ED fosforila\u010Dn\u00ED (P)-dom\u00E9ny nen\u00ED nezbytn\u00E1 pro v\u00E1z\u00E1n\u00ED TNP-ATP. Nem\u00E1me \u017E\u00E1dn\u00E9 n\u00E1znaky o druh\u00E9m vazebn\u00EDm m\u00EDst\u011B ATP na P-dom\u00E9n\u011B isolovan\u00E9 kli\u010Dky, p\u0159esto\u017Ee jin\u00ED d\u0159\u00EDva psali o jeho existenci pomoc\u00ED TNP-N3ADP afinitn\u00EDm zna\u010Den\u00EDm cel\u00E9ho enzymu. Fluorescein isothiocyanate (FITC)-anizotropn\u00ED m\u011B\u0159en\u00ED uk\u00E1zala zna\u010Dnou stabilitu nukleotidov\u00E9 (N)-dom\u00E9ny, co\u017E nazna\u010Duje, \u017Ee tato dom\u00E9na neproch\u00E1z\u00ED podstatn\u00FDmi konforma\u010Dn\u00EDmi zm\u011Bnami p\u0159i v\u00E1z\u00E1n\u00ED ATP. FITCem modifikovan\u00E1 kli\u010Dka uk\u00E1zala pouze slab\u011B zmen\u0161enou fosfat\u00E1zovou aktivitu, s nejv\u011Bt\u0161\u00ED pravd\u011Bpodobnost\u00ED kv\u016Fli pNPP vazebn\u00EDmu m\u00EDstu na N-dom\u00E9n\u011B kolem N398, jeho\u017E mutace na D sn\u00ED\u017Eily fosfat\u00E1zovou aktivitu o 50 %. Aminokyseliny vytv\u00E1\u0159ej\u00EDc\u00ED toto vazebn\u00E9 m\u00EDsto pro pNPP (M38..."@cs . "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..." . "The phosphatase activity of the isolated H4-H5 loop of Na+/K+ ATPase resides outside its ATP binding site"@en . "phosphatase"@en . "579377" . . "European Journal of Biochemistry" . "271" . . "Fosfat\u00E1zov\u00E1 aktivita isolovan\u00E9 H4-H5 kli\u010Dky z Na+/K+ ATP\u00E1zy se nach\u00E1z\u00ED mimo vazebn\u00E9 m\u00EDsto pro ATP"@cs . "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 . . "P(GA204/01/0254), P(GA204/01/1001), P(GA309/02/1479), P(GP206/03/D082), P(LN00A141), Z(AV0Z5011922)" . "The phosphatase activity of the isolated H4-H5 loop of Na+/K+ ATPase resides outside its ATP binding site" . "17"^^ . . "0014-2956" . . "RIV/67179843:_____/04:00031718" . "Ettrich, R\u00FCdiger" . "The phosphatase activity of the isolated H4-H5 loop of Na+/K+ ATPase resides outside its ATP binding site"@en . "3923;3939" . . "Fosfat\u00E1zov\u00E1 aktivita isolovan\u00E9 H4-H5 kli\u010Dky z Na+/K+ ATP\u00E1zy se nach\u00E1z\u00ED mimo vazebn\u00E9 m\u00EDsto pro ATP"@cs . . . "1"^^ .