Backbone NMR resonance assignment of the catalytic subunit of cAMP-dependent protein kinase A in complex with AMP-PNP

Larry R. Masterson, Lei Shi, Marco Tonelli, Alessandro Mascioni, Michael M. Mueller, Gianluigi Veglia

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

Abstract

The catalytic subunit of protein kinase A is involved with a number of signal transduction pathways and has been used as a benchmark to study the structural biology and biochemistry for the entire kinase family of enzymes. Here, we report the backbone assignment of the intact 41 kDa catalytic subunit bound to AMP-PNP.

Original languageEnglish (US)
Pages (from-to)115-117
Number of pages3
JournalBiomolecular NMR Assignments
Volume3
Issue number1
DOIs
StatePublished - Jun 2009

Bibliographical note

Funding Information:
Acknowledgments This work was supported by NIH grants GM64742 and HL080081 (G.V.), and GM08700 (L.R.M.). The University of Minnesota NMR facility is supported by NSF funding BIR-961477 and the University of Minnesota Medical Foundation. NMRFAM is supported by NIH grants P41RR02301, P41GM66326, RR02781, and RR08438, along with NSF grants DMB-8415048, OIA-9977486, and BIR-9214394.

Keywords

  • CCLS-HSQC
  • Dual amino acid selective labeling
  • NMR
  • Protein backbone resonance assignments
  • Protein kinase A

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