dc.creatorJung, Stephan
dc.creatorHoffmann, Ralf
dc.creatorRodriguez, Patricio H.
dc.creatorMutzel, Rupert
dc.creatorHofer, Hans Werner
dc.date.accessioned2019-01-29T14:55:21Z
dc.date.available2019-01-29T14:55:21Z
dc.date.created2019-01-29T14:55:21Z
dc.date.issued1995
dc.identifierEuropean Journal of Biochemistry, Volumen 232, Issue 1, 2018, Pages 111-117
dc.identifier14321033
dc.identifier00142956
dc.identifier10.1111/j.1432-1033.1995.tb20788.x
dc.identifierhttps://repositorio.uchile.cl/handle/2250/161344
dc.description.abstractA complete cDNA clone encoding the catalytic subunit of cAMP‐dependent protein kinase of Ascaris suum was constructed from two overlapping partial clones. The encoded sequence of 337 ammo acids is 48 % identical with the sequence of mouse Cα subunit. Approximately the same low similarity was found with the sequence of the C subunit from another nematode, Caenorhabditis elegans. The N‐terminal 14 amino acids and the myristoylation site of the mammalian protein are not contained in the enzyme from Ascaris. Two cysteines (Cys33 and Cys319) replace a basic residue in the N‐terminal region and an acidic amino acid near the C‐terminus which are conserved in all known C subunits from other sources. The substitutions provide the possibility of disulfide bridge formation between the N‐terminal and C‐terminal parts of the protein. There is strong evidence that a single gene encodes cAMP‐dependent protein kinase in Ascaris. Modelling of the sequence into the coordinates of the X‐ray structure of
dc.languageen
dc.rightshttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
dc.sourceEuropean Journal of Biochemistry
dc.subjectAscaris
dc.subjectnematode
dc.subjectprotein kinase (PkA)
dc.subjectprotein kinase A sequence
dc.subjectstructural modelling
dc.titleThe Catalytic Subunit of cAMP‐Dependent Protein Kinase from Ascaris suum The Cloning and Structure of a Novel Subtype of Protein Kinase A
dc.typeArtículo de revista


Este ítem pertenece a la siguiente institución