FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2024235333> ?p ?o ?g. }

• W2024235333 endingPage "1920" @default.
• W2024235333 startingPage "1908" @default.
• W2024235333 abstract "Although individual structures of cAMP-dependent protein kinase (PKA) catalytic (C) and regulatory (R) subunits have been determined at the atomic level, our understanding of the effects of cAMP activation on protein dynamics and intersubunit communication of PKA holoenzymes is very limited. To delineate the mechanism of PKA activation and structural differences between type I and II PKA holoenzymes, the conformation and structural dynamics of PKA holoenzymes Ialpha and IIbeta were probed by amide hydrogen-deuterium exchange coupled with Fourier transform infrared spectroscopy (FT-IR) and chemical protein footprinting. Binding of cAMP to PKA holoenzymes Ialpha and IIbeta leads to a downshift in the wavenumber for both the alpha-helix and beta-strand bands, suggesting that R and C subunits become overall more dynamic in the holoenzyme complexes. This is consistent with the H-D exchange results showing a small change in the overall rate of exchange in response to the binding of cAMP to both PKA holoenzymes Ialpha and IIbeta. Despite the overall similarity, significant differences in the change of FT-IR spectra in response to the binding of cAMP were observed between PKA holoenzymes Ialpha and IIbeta. Activation of PKA holoenzyme Ialpha led to more conformational changes in beta-strand structures, while cAMP induced more apparent changes in the alpha-helical structures in PKA holoenzyme IIbeta. Chemical protein footprinting experiments revealed an extended docking surface for the R subunits on the C subunit. Although the overall subunit interfaces appeared to be similar for PKA holoenzymes Ialpha and IIbeta, a region around the active site cleft of the C subunit was more protected in PKA holoenzyme Ialpha than in PKA holoenzyme IIbeta. These results suggest that the C subunit assumes a more open conformation in PKA holoenzyme IIbeta. In addition, the chemical cleavage patterns around the active site cleft of the C subunit were distinctly different in PKA holoenzymes Ialpha and IIbeta even in the presence of cAMP. These observations provide direct evidence that the R subunits may be partially associated with the C subunit with the pseudosubstrate sequence docked in the active site cleft in the presence of cAMP." @default.
• W2024235333 created "2016-06-24" @default.
• W2024235333 creator A5041893418 @default.
• W2024235333 creator A5064997314 @default.
• W2024235333 creator A5076097117 @default.
• W2024235333 creator A5080619609 @default.
• W2024235333 date "2004-01-29" @default.
• W2024235333 modified "2023-10-01" @default.
• W2024235333 title "Probing cAMP-Dependent Protein Kinase Holoenzyme Complexes Iα and IIβ by FT-IR and Chemical Protein Footprinting" @default.
• W2024235333 cites W1504222076 @default.
• W2024235333 cites W1554141309 @default.
• W2024235333 cites W1575835136 @default.
• W2024235333 cites W1589638018 @default.
• W2024235333 cites W1625449763 @default.
• W2024235333 cites W1968481822 @default.
• W2024235333 cites W1979033389 @default.
• W2024235333 cites W1992905023 @default.
• W2024235333 cites W2006382951 @default.
• W2024235333 cites W2020257412 @default.
• W2024235333 cites W2024229820 @default.
• W2024235333 cites W2049502625 @default.
• W2024235333 cites W2051323583 @default.
• W2024235333 cites W2052359072 @default.
• W2024235333 cites W2074312161 @default.
• W2024235333 cites W2101652741 @default.
• W2024235333 cites W2107006579 @default.
• W2024235333 cites W2125141239 @default.
• W2024235333 cites W2141524439 @default.
• W2024235333 doi "https://doi.org/10.1021/bi0354435" @default.
• W2024235333 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/14967031" @default.
• W2024235333 hasPublicationYear "2004" @default.
• W2024235333 type Work @default.
• W2024235333 sameAs 2024235333 @default.
• W2024235333 citedByCount "14" @default.
• W2024235333 countsByYear W20242353332012 @default.
• W2024235333 countsByYear W20242353332013 @default.
• W2024235333 countsByYear W20242353332015 @default.
• W2024235333 countsByYear W20242353332020 @default.
• W2024235333 crossrefType "journal-article" @default.
• W2024235333 hasAuthorship W2024235333A5041893418 @default.
• W2024235333 hasAuthorship W2024235333A5064997314 @default.
• W2024235333 hasAuthorship W2024235333A5076097117 @default.
• W2024235333 hasAuthorship W2024235333A5080619609 @default.
• W2024235333 hasConcept C104292427 @default.
• W2024235333 hasConcept C104317684 @default.
• W2024235333 hasConcept C12554922 @default.
• W2024235333 hasConcept C181199279 @default.
• W2024235333 hasConcept C185592680 @default.
• W2024235333 hasConcept C2778021871 @default.
• W2024235333 hasConcept C55493867 @default.
• W2024235333 hasConcept C86339819 @default.
• W2024235333 hasConcept C86803240 @default.
• W2024235333 hasConcept C97029542 @default.
• W2024235333 hasConceptScore W2024235333C104292427 @default.
• W2024235333 hasConceptScore W2024235333C104317684 @default.
• W2024235333 hasConceptScore W2024235333C12554922 @default.
• W2024235333 hasConceptScore W2024235333C181199279 @default.
• W2024235333 hasConceptScore W2024235333C185592680 @default.
• W2024235333 hasConceptScore W2024235333C2778021871 @default.
• W2024235333 hasConceptScore W2024235333C55493867 @default.
• W2024235333 hasConceptScore W2024235333C86339819 @default.
• W2024235333 hasConceptScore W2024235333C86803240 @default.
• W2024235333 hasConceptScore W2024235333C97029542 @default.
• W2024235333 hasIssue "7" @default.
• W2024235333 hasLocation W20242353331 @default.
• W2024235333 hasLocation W20242353332 @default.
• W2024235333 hasOpenAccess W2024235333 @default.
• W2024235333 hasPrimaryLocation W20242353331 @default.
• W2024235333 hasRelatedWork W1971050671 @default.
• W2024235333 hasRelatedWork W1980598737 @default.
• W2024235333 hasRelatedWork W1993253042 @default.
• W2024235333 hasRelatedWork W2024098505 @default.
• W2024235333 hasRelatedWork W2024691506 @default.
• W2024235333 hasRelatedWork W2027768367 @default.
• W2024235333 hasRelatedWork W2092461227 @default.
• W2024235333 hasRelatedWork W2098038478 @default.
• W2024235333 hasRelatedWork W2754155872 @default.
• W2024235333 hasRelatedWork W41731184 @default.
• W2024235333 hasVolume "43" @default.
• W2024235333 isParatext "false" @default.
• W2024235333 isRetracted "false" @default.
• W2024235333 magId "2024235333" @default.
• W2024235333 workType "article" @default.