The intrinsically disordered C terminus of troponin T binds to troponin C to modulate myocardial force generation.
Binding Sites
Calcium
/ metabolism
Cardiomyopathy, Dilated
/ metabolism
Female
Humans
Male
Mutagenesis, Site-Directed
Myocardial Contraction
Myocardium
/ metabolism
Myofibrils
/ physiology
Nuclear Magnetic Resonance, Biomolecular
Pedigree
Protein Binding
Protein Domains
Protein Structure, Secondary
Troponin C
/ chemistry
Troponin T
/ chemistry
NMR
cardiac muscle
cardiomyopathy
cardiovascular disease
contractile protein
cross-bridges
protein dynamic
structure–function
troponin
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
27 12 2019
27 12 2019
Historique:
received:
19
09
2019
revised:
13
11
2019
pubmed:
22
11
2019
medline:
23
6
2020
entrez:
22
11
2019
Statut:
ppublish
Résumé
Aberrant regulation of myocardial force production represents an early biomechanical defect associated with sarcomeric cardiomyopathies, but the molecular mechanisms remain poorly defined. Here, we evaluated the pathogenicity of a previously unreported sarcomeric gene variant identified in a pediatric patient with sporadic dilated cardiomyopathy, and we determined a molecular mechanism. Trio whole-exome sequencing revealed a
Identifiants
pubmed: 31748410
pii: S0021-9258(20)30025-9
doi: 10.1074/jbc.RA119.011177
pmc: PMC6937556
doi:
Substances chimiques
Troponin C
0
Troponin T
0
Calcium
SY7Q814VUP
Banques de données
PDB
['1J1E']
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
20054-20069Subventions
Organisme : NHLBI NIH HHS
ID : R01 HL128683
Pays : United States
Informations de copyright
© 2019 Johnston et al.
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