Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structure of the unliganded cAMP-dependent protein kinase catalytic subunit from Saccharomyces cerevisiae.

Archives of biochemistry and biophysics - 1 Mar 2001

Mashhoon N, Carmel G, Pflugrath J W, Kuret J

Abstract excerpt

The structure of TPK1delta, a truncated variant of the cAMP-dependent protein kinase catalytic subunit from Saccharomyces cerevisiae, was determined in an unliganded state at 2.8 A resolution and refined to a crystallographic R-factor of 19.4%. Comparison of this structure to that of its fully li...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Catalysis
Share to Catalytic Domain
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cyclic AMP-Dependent Protein Kinases

Share to Ligands

Share to Peptide Fragments

Share to Protein Subunits

Share to Substrate Specificity

Source

Identifiers

PMID: 11368172
DOI: 10.1006/abbi.2000.2241

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026. Prepared record publication-11368172-2026-08-31.1. Manifest publication-graph-cohort-2026-08-31.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 31 Aug 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 9 closest

Structure of the unliganded cAMP-dependent protein kinase catalytic subunit from Saccharomyces cerevisiae.PMID 11368172Read ↗

A template for the protein kinase family.Semantic proximity Read ↗

Catalytic independent functions of a protein kinase as revealed by a kinase-dead mutant: study of the Lys72His mutant of cAMP-dependent kinase.Semantic proximity Read ↗

Systematic mutational analysis of cAMP-dependent protein kinase identifies unregulated catalytic subunits and defines regions important for the recognition of the regulatory subunit.Semantic proximity Read ↗

Crystal structure of a cAMP-dependent protein kinase mutant at 1.26A: new insights into the catalytic mechanism.Semantic proximity Read ↗

Regulatory subunit of protein kinase A: structure of deletion mutant with cAMP binding domains.Semantic proximity Read ↗

[Purification and characterization of cAMP-dependent protein kinases of yeasts in a Saccharomyces cerevisiae wild strain and selected mutants of cAMP metabolism].Semantic proximity Read ↗

Nature and transcriptional role of catalytic subunits of yeast mitochondrial cAMP-dependent protein kinase.Semantic proximity Read ↗

Crystal structure of the S. cerevisiae D-ribose-5-phosphate isomerase: comparison with the archaeal and bacterial enzymes.Semantic proximity Read ↗

Dissecting the domain structure of the regulatory subunit of cAMP-dependent protein kinase I and elucidating the role of MgATP.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.