Magyar
Toggle navigation
Tudóstér
Magyar
Tudóstér
Keresés
Egyszerű keresés
Összetett keresés
CCL keresés
Egyszerű keresés
Összetett keresés
CCL keresés
Böngészés
Saját polc tartalma
(
0
)
Korábbi keresések
Összesen 1 találat.
#/oldal:
12
36
60
120
Rövid
Hosszú
MARC
Részletezés:
Rendezés:
Szerző növekvő
Szerző csökkenő
Cím növekvő
Cím csökkenő
Dátum növekvő
Dátum csökkenő
1.
001-es BibID:
BIBFORM005284
Első szerző:
Kövér Katalin, E. (vegyész)
Cím:
The solution structure and dynamics of human pancreatic ribonuclease determined by NMR spectroscopy provide insight into its remarkable biological activities and inhibition / K. E. Kövér, M. Bruix, J. Santoro, G. Batta, D. V. Laurents and M. Rico
Dátum:
2008
Megjegyzések:
Human pancreatic ribonuclease (RNase 1) is expressed in many tissues; has several important enzymatic and biological activities, including efficient cleavage of single-stranded RNA, double-stranded RNA and double-stranded RNA-DNA hybrids, digestion of dietary RNA, regulation of vascular homeostasis, inactivation of the HIV, activation of immature dendritic cells and induction of cytokine production; and furthermore shows potential as an anti-tumor agent. The solution structure and dynamics of uncomplexed, wild-type RNase 1 have been determined by NMR spectroscopy methods to better understand these activities. The family of 20 structures determined on the basis of 6115 unambiguous nuclear Over hauser enhancements is well resolved (pairwise backbone RMSD = 1.07 angstrom) and has the classic RNase A type of tertiary structure. Important structural differences compared with previously determined crystal structures of RNase 1 variants or inhibitor-bound complexes ate observed in the conformation of loop regions and side chains implicated in the enzymatic as well as biological activities and binding to the cytoplasmic RNase inhibitor. Multiple side chain conformations observed for key surface residues are proposed to be crucial for membrane binding as well as translocation and efficient RNA hydrolysis. N-15-H-1 relaxation measurements interpreted with the standard and our extended Lipari-Szabo formalism reveal rigid regions and identify more dynamic loop regions. Some of the most dynamic areas are key for binding to the cytoplasmic RNase inhibitor. This finding and the important differences observed between the structure in solution and that bound to the inhibitor are indications that RNase 1 to inhibitor binding can be better described by the "induced fit" model rather than the rigid "lock-into-key" mechanism. Translational diffusion measurements reveal that RNase 1 is predominantly dimeric above 1 mM concentration; the possible implications of this dimeric state for the remarkable biological properties of RNase 1 are discussed.
Tárgyszavak:
Természettudományok
Fizikai tudományok
idegen nyelvű folyóiratközlemény külföldi lapban
Human pancreatic ribonuclease
Megjelenés:
Journal of Molecular Biology. - 379 : 5 (2008), p. 953-965. -
További szerzők:
Bruix, Marta
Santoro, J.
Batta Gyula (1953-) (molekula-szerkezet kutató)
Laurents, Douglas V.
Rico, M.
Internet cím:
elektronikus változat
Borító:
Saját polcon:
Rekordok letöltése
1
Corvina könyvtári katalógus v8.2.27
© 2023
Monguz kft.
Minden jog fenntartva.