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001-es BibID:	BIBFORM003012
Első szerző:	Groves, Patrick
Cím:	Temperature dependence of ligand-protein complex formation as reflected by saturation transfer difference NMR experiments / Patrick Groves, Katalin E. Kövér, Sabine André, Joanna Bandorowicz-Pikula, Gyula Batta, Marta Bruix, René Buchet, Angeles Canales, F. Javier Canada, Hans-Joachim Gabius, Douglas V. Laurents, Jose R. Naranjo, Małgorzata Palczewska, Slawomir Pikula, Eduardo Rial, Agnieszka Strzelecka-Kiliszek and Jesús Jiménez-Barbero
Dátum:	2007
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Magnetic Resonance In Chemistry. - 45 : 9 (2007), p. 745-748 -
További szerzők:	Kövér Katalin, E. (1956-2023) (vegyész) André, Sabine Bandorowicz-Pikula, Joanna Batta Gyula (1953-) (molekula-szerkezet kutató) Bruix, Marta Buchet, René Canales, Angeles Canada, F. Javier Gabius, Hans-Joachim Laurents, Douglas V. Naranjo, Jose R. Palczewska, Małgorzata Pikula, Slawomir Rial, Eduardo Strzelecka-Kiliszek, Agnieszka Jiménez-Barbero, Jesús
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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.
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