Interaction of Protein Kinase Ac from Ascaris suum with Proteins and Peptides: Comparison with the Mammalian Enzyme View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1997

AUTHORS

S. Jung , R. Hoffmann , T. Treptau , P. H. Rodriguez , B. G. Harris , P. F. Cook , H. W. Hofer

ABSTRACT

Protein kinases belong to a single large family of proteins (Hanks et al., 1988) and exhibit considerable similarity in primary and tertiary structure. While they are highly specific for ATP as phosphate donor (only a small minority uses GTP as an alternative), their limited in vitro specificity for protein substrates is remarkable with regard to the specialized functions of protein kinases in signal transduction, and cellular and metabolic regulation. Most obvious specificities attributed to certain subfamilies concern their ability to catalyze the formation of phosphate esters of either aliphatic or aromatic amino acid residues (or both) and the requirement for given recognition sites. Typically, these recognition sites are degenerate and comprise only a few amino acids in the vicinity of a serine, threonine or tyrosine residue, thus hardly providing elaborate tools of molecular recognition. More... »

PAGES

19-24

Book

TITLE

Interacting Protein Domains

ISBN

978-3-642-64583-9
978-3-642-60848-3

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-3-642-60848-3_4

DOI

http://dx.doi.org/10.1007/978-3-642-60848-3_4

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1024556224


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