"0"^^ . "Molekul\u00E1rn\u00ED mechanismus interakce mezi H4-H5 smy\u010Dkou Na+/K+-ATP\u00E1zy a vazebn\u00FDm m\u00EDstem pro srde\u010Dn\u00ED glykosidy" . "1"^^ . "Na+/K+-ATP\u00E1za je transportn\u00EDm enzymem pro sod\u00EDk a drasl\u00EDk p\u0159es plazmatickou membr\u00E1nu, kter\u00FD je v\u0161ak z\u00E1rove\u0148 naz\u00FDv\u00E1n receptorem srde\u010Dn\u00EDch glykozid\u016F. Vazebn\u00E9 m\u00EDsto pro srde\u010Dn\u00ED glykozidy je v\u0161ak lokjalizov\u00E1no relativn\u011B daleko od vazebn\u00E9ho m\u00EDsta pro ATP. Tato vazebn\u00E1 m\u00EDsta v\u0161ak zcela z\u0159ejm\u011B kooperuj\u00ED. Podle ned\u00E1vn\u00FDch zji\u0161t\u011Bn\u00ED koexistuj\u00ED ve funk\u010Dn\u00EDm enzymov\u00E9m komplexu vysokoafinn\u00ED (E1) a n\u00EDzkoafinn\u00ED (E2) vazebn\u00E1 m\u00EDsta pro ATP, nen\u00ED v\u0161ak dosud z\u0159ejm\u00E9, zda jsou odli\u0161n\u00E1 \u010Di projevem r\u016Fzn\u00FDch efinit jednoho m\u00EDsta. Specifick\u00FDm c\u00EDlem navrhovan\u00E9 studie je: 1) izolovat a krystalizovat H4-H5 smy\u010Dku, 2) ur\u010Dit sekund\u00E1rn\u00ED strukturu transmembr\u00E1nov\u00FDch segment\u016F alfa-podjednotky, 3) ur\u010Dit sekund\u00E1rn\u00ED a terci\u00E1rn\u00ED strukturu H4-H5 smy\u010Dky a srovnat ji s nativn\u00EDm komplexem, 4) lokalizovat vazebn\u00E9 m\u00EDsto pro srde\u010Dn\u00ED glykozidy." . . . . "7"^^ . . "7"^^ . "Molecular mechanism of interaction between the H4-H5 loop of Na+/K+-ATPase and the binding site for cardiac glycosides"@en . "Exprese a purifikace cytoplazmat. dom\u00E9ny Na,K-ATP\u00E1zy s ATP vazebn\u00FDm m\u00EDstem v\u010D. jej\u00EDch mutant. Lokalizace ATP vazebn\u00FDch m\u00EDst a d\u016Fkaz funk\u010Dn\u00EDho dimeru Na,K-ATP\u00E1zy. Vytvo\u0159en\u00ED alternativn\u00EDho modelu k Albers-Postovu schematu."@cs . "http://www.isvav.cz/projectDetail.do?rowId=IAA7011801"^^ . . "IAA7011801" . . . . . . . . . . . "Na+/K+-ATPase is transporting enzyme for Na+ and K+ across the plasma membrane which is also called a receptor for cardioactive glycosides. The binding site for cardiac glycosides was revealed to be far away from the binding site for ATP. These binding sites, however, apparently cooperate. As revealed recently, the high (E1) and low (E2) affinity ATP binding sites coexist at the functional Na+/K+ complex. There is not clear, yet, whether one binding site has different affinities during the transport cycle or whether two different binding sites coexist at the hughe H4-H5 loop of the alpha-subunit. The specific aims of the proposed study are: 1)to isolate and crystallize the H4-H5 loop to find out whether it preserves its affinity to ATP analogs, 2) to determine the secondary structure of the transmembrane segments of the aplha-subunit, 3) to determine the secondary and tertiary structures of the native H4-H5 loop and compare them with the isolated segment."@en . "0"^^ .