› 1vdi

Solution NMR

Solution structure of actin-binding domain of troponin in Ca2+-free state

Released:
DOI: 10.2210/pdb1vdi/pdb
PDB entry 1vdi coloured by chain, ensemble of 20 models, front view.
PDB entry 1vdi coloured by chain, ensemble of 20 models, side view.
PDB entry 1vdi coloured by chain, ensemble of 20 models, top view.
Source organism: Gallus gallus
Primary publication:
Structural basis for Ca2+-regulated muscle relaxation at interaction sites of troponin with actin and tropomyosin.
Murakami K, Yumoto F, Ohki SY, Yasunaga T, Tanokura M, Wakabayashi T
J Mol Biol 352 178-201 (2005)
PMID: 16061251

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159359 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Troponin I, fast skeletal muscle Chain: A
Molecule details ›
Chain: A
Length: 52 amino acids
Theoretical weight: 6.14 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli
UniProt:
  • Canonical: P68246 (Residues: 132-183; Coverage: 28%)
Gene name: TNNI2
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Escherichia coli

Quick links

Citations

17 review citations

The unique functions of cardiac troponin I in the control of cardiac muscle contraction and relaxation.
Solaro et al. (2008)
16 more

3 mentions without citation

Structural basis for calcium-regulated relaxation of striated muscles at interaction sites of troponin with actin and tropomyosin.
Murakami et al. (2007)
2 more