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High-resolution crystal structure of cAMP-dependent protein kinase from Cricetulus griseus.

Kudlinzki D, Linhard VL, Saxena K, Sreeramulu S, Gande S, Schieborr U, Dreyer M, Schwalbe H
Acta Crystallogr F Struct Biol Commun 71 1088-93 (2015)
Cited: 3 times
EuropePMC logo PMID: 26249705

Abstract

Protein kinases (PKs) are dynamic regulators of numerous cellular processes. Their phosphorylation activity is determined by the conserved kinase core structure, which is maintained by the interaction and dynamics with associated domains or interacting proteins. The prototype enzyme for investigations to understand the activity and regulation of PKs is the catalytic subunit of cAMP-dependent protein kinase (PKAc). Major effects of functional regulation and ligand binding are driven by only minor structural modulations in protein-protein interactions. In order to resolve such minor structural differences, very high resolution structures are required. Here, the high-resolution X-ray structure of PKAc from Cricetulus griseus is reported.

Articles - 4wih mentioned but not cited (1)

  1. High-resolution crystal structure of cAMP-dependent protein kinase from Cricetulus griseus. Kudlinzki D, Linhard VL, Saxena K, Sreeramulu S, Gande S, Schieborr U, Dreyer M, Schwalbe H. Acta Crystallogr F Struct Biol Commun 71 1088-1093 (2015)


Articles citing this publication (2)

  1. Two Methods, One Goal: Structural Differences between Cocrystallization and Crystal Soaking to Discover Ligand Binding Poses. Wienen-Schmidt B, Oebbeke M, Ngo K, Heine A, Klebe G. ChemMedChem 16 292-300 (2021)
  2. Diamondoid Amino Acid-Based Peptide Kinase A Inhibitor Analogues. Müller J, Kirschner RA, Berndt JP, Wulsdorf T, Metz A, Hrdina R, Schreiner PR, Geyer A, Klebe G. ChemMedChem 14 663-672 (2019)


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