Dynamical characterization of the heme NO oxygen binding (HNOX) domain. Insight into soluble guanylate cyclase allosteric transition

Since the discovery of soluble guanylate cyclase (sGC) as the mammalian receptor for nitric oxide (NO), numerous studies have been performed in order to understand how sGC transduces the NO signal. However, the structural basis of sGC activation is still not completely elucidated. Spectroscopic and...

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Detalles Bibliográficos
Autores principales:	Capece, Luciana, Estrin, Dario Ariel, Martí, Marcelo Adrián
Publicado:	2008
Materias:	Biochemistry Computational methods Computer networks Computer simulation Mammals Mechanisms Nitric oxide Oxygen Proteins Activation mechanisms Soluble guanylate cyclase Hemoglobin guanylate cyclase hemoprotein histidine allosterism article computer simulation enzyme activation heme nitric oxide oxygen binding ligand binding priority journal protein conformation protein domain protein structure spectroscopy Thermoanaerobacter thermoanaerobacter tencogensis Allosteric Regulation Animals Bacterial Proteins Computer Simulation Enzyme Activation Guanylate Cyclase Heme Histidine Humans Iron Models, Molecular Nitric Oxide Protein Binding Protein Structure, Secondary Protein Structure, Tertiary Signal Transduction Structure-Activity Relationship Mammalia Prokaryota
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00062960_v47_n36_p9416_Capece http://hdl.handle.net/20.500.12110/paper_00062960_v47_n36_p9416_Capece
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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