FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2017659051> ?p ?o ?g. }

• W2017659051 endingPage "2911" @default.
• W2017659051 startingPage "2902" @default.
• W2017659051 abstract "The interaction between the calcium binding and inhibitory components of troponin is central to the regulation of muscle contraction. In this work, two-dimensional heteronuclear single-quantum coherence nuclear magnetic resonance (2D-{1H,15N}-HSQC NMR) spectroscopy was used to determine the stoichiometry, affinity, and mechanisms for binding of Ca2+ and two synthetic TnI peptides [TnI1-40 (or Rp40) and TnI96-115] to the isolated C-domain of skeletal troponin C (CTnC). The Ca2+ titration revealed that 2 equiv of Ca2+ binds to sites III and IV of CTnC with strong positive cooperativity and high affinity [dissociation constant (KD) ≤ 0.1 μM]. In this process, CTnC folds from a largely unstructured state to a compact domain capable of interacting with TnI. Titration of CTnC·2Ca2+ with Rp40 occurs with a 1:1 stoichiometry and a KD of 2 ± 1 μM. Titration of CTnC·2Ca2+ with a peptide corresponding to the inhibitory region of TnI (TnI96-115) also reveals a 1:1 ratio, but weaker affinity (KD = 47 ± 7 μM). Both Rp40- and TnI96-115-induced backbone amide chemical shift changes of CTnC·2Ca2+ are similarly distributed along the sequence, indicating that these two regions of TnI may compete for the same binding site on CTnC·2Ca2+. The changes induced by Rp40 are much larger, however, and define the interaction sites on TnC and regions where the flexibility of hinge and terminal residues is altered. To investigate the possibility of direct competition, TnI96-115 was titrated into the CTnC·2Ca2+·Rp40 complex, whereas Rp40 was titrated into the CTnC·2Ca2+·TnI96-115 complex. The results show that Rp40 can displace TnI96-115 completely, while TnI96-115 has no effect on CTnC·2Ca2+·Rp40. Recent proposals for the mechanism of muscle regulation [Tripet, B. P., Van Eyk, J. E., and Hodges, R. S. (1997) J. Mol. Biol. 271, 728−750] suggest that the N-terminal and inhibitory regions of TnI competitively bind the structural domain of TnC. The findings presented here indicate that additional factors, such as interactions between the N-domain of TnC with the C-domain of TnI or the C-domain of TnT, are required, if the inhibitory region is going to successfully compete for the structural domain of TnC." @default.
• W2017659051 created "2016-06-24" @default.
• W2017659051 creator A5067477469 @default.
• W2017659051 creator A5068205700 @default.
• W2017659051 creator A5085091631 @default.
• W2017659051 date "2000-02-22" @default.
• W2017659051 modified "2023-10-14" @default.
• W2017659051 title "Role of the Structural Domain of Troponin C in Muscle Regulation: NMR Studies of Ca²⁺ Binding and Subsequent Interactions with Regions 1−40 and 96−115 of Troponin I" @default.
• W2017659051 cites W1550330933 @default.
• W2017659051 cites W1554913126 @default.
• W2017659051 cites W1747748421 @default.
• W2017659051 cites W1810428052 @default.
• W2017659051 cites W1848560850 @default.
• W2017659051 cites W1954284565 @default.
• W2017659051 cites W1974327668 @default.
• W2017659051 cites W1975475509 @default.
• W2017659051 cites W1985322317 @default.
• W2017659051 cites W1992679398 @default.
• W2017659051 cites W1998856157 @default.
• W2017659051 cites W2017827510 @default.
• W2017659051 cites W2018531588 @default.
• W2017659051 cites W2030433731 @default.
• W2017659051 cites W2037342659 @default.
• W2017659051 cites W2045950270 @default.
• W2017659051 cites W2093647723 @default.
• W2017659051 cites W2096716204 @default.
• W2017659051 cites W2099152212 @default.
• W2017659051 cites W2110591420 @default.
• W2017659051 cites W2121049846 @default.
• W2017659051 cites W2169821755 @default.
• W2017659051 cites W2175328062 @default.
• W2017659051 cites W2412059871 @default.
• W2017659051 cites W2949250147 @default.
• W2017659051 doi "https://doi.org/10.1021/bi992579n" @default.
• W2017659051 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10715110" @default.
• W2017659051 hasPublicationYear "2000" @default.
• W2017659051 type Work @default.
• W2017659051 sameAs 2017659051 @default.
• W2017659051 citedByCount "41" @default.
• W2017659051 countsByYear W20176590512014 @default.
• W2017659051 countsByYear W20176590512015 @default.
• W2017659051 countsByYear W20176590512016 @default.
• W2017659051 countsByYear W20176590512017 @default.
• W2017659051 countsByYear W20176590512021 @default.
• W2017659051 countsByYear W20176590512022 @default.
• W2017659051 crossrefType "journal-article" @default.
• W2017659051 hasAuthorship W2017659051A5067477469 @default.
• W2017659051 hasAuthorship W2017659051A5068205700 @default.
• W2017659051 hasAuthorship W2017659051A5085091631 @default.
• W2017659051 hasConcept C107824862 @default.
• W2017659051 hasConcept C115725540 @default.
• W2017659051 hasConcept C118552586 @default.
• W2017659051 hasConcept C12554922 @default.
• W2017659051 hasConcept C133927893 @default.
• W2017659051 hasConcept C15744967 @default.
• W2017659051 hasConcept C166014724 @default.
• W2017659051 hasConcept C170493617 @default.
• W2017659051 hasConcept C179104552 @default.
• W2017659051 hasConcept C184866935 @default.
• W2017659051 hasConcept C185592680 @default.
• W2017659051 hasConcept C193125475 @default.
• W2017659051 hasConcept C500558357 @default.
• W2017659051 hasConcept C55493867 @default.
• W2017659051 hasConcept C66974803 @default.
• W2017659051 hasConcept C71240020 @default.
• W2017659051 hasConcept C74998103 @default.
• W2017659051 hasConcept C8010536 @default.
• W2017659051 hasConcept C86803240 @default.
• W2017659051 hasConceptScore W2017659051C107824862 @default.
• W2017659051 hasConceptScore W2017659051C115725540 @default.
• W2017659051 hasConceptScore W2017659051C118552586 @default.
• W2017659051 hasConceptScore W2017659051C12554922 @default.
• W2017659051 hasConceptScore W2017659051C133927893 @default.
• W2017659051 hasConceptScore W2017659051C15744967 @default.
• W2017659051 hasConceptScore W2017659051C166014724 @default.
• W2017659051 hasConceptScore W2017659051C170493617 @default.
• W2017659051 hasConceptScore W2017659051C179104552 @default.
• W2017659051 hasConceptScore W2017659051C184866935 @default.
• W2017659051 hasConceptScore W2017659051C185592680 @default.
• W2017659051 hasConceptScore W2017659051C193125475 @default.
• W2017659051 hasConceptScore W2017659051C500558357 @default.
• W2017659051 hasConceptScore W2017659051C55493867 @default.
• W2017659051 hasConceptScore W2017659051C66974803 @default.
• W2017659051 hasConceptScore W2017659051C71240020 @default.
• W2017659051 hasConceptScore W2017659051C74998103 @default.
• W2017659051 hasConceptScore W2017659051C8010536 @default.
• W2017659051 hasConceptScore W2017659051C86803240 @default.
• W2017659051 hasIssue "11" @default.
• W2017659051 hasLocation W20176590511 @default.
• W2017659051 hasLocation W20176590512 @default.
• W2017659051 hasOpenAccess W2017659051 @default.
• W2017659051 hasPrimaryLocation W20176590511 @default.
• W2017659051 hasRelatedWork W2004189116 @default.
• W2017659051 hasRelatedWork W2017241272 @default.
• W2017659051 hasRelatedWork W2044848803 @default.
• W2017659051 hasRelatedWork W2079486238 @default.
• W2017659051 hasRelatedWork W2079558267 @default.
• W2017659051 hasRelatedWork W2159652526 @default.

• next