› 2l3l

Solution NMR

The solution structure of the N-terminal domain of human Tubulin Binding Cofactor C reveals a platform for the interaction with ab-tubulin

Released:
DOI: 10.2210/pdb2l3l/pdb
PDB entry 2l3l coloured by chain, ensemble of 20 models, front view.
PDB entry 2l3l coloured by chain, ensemble of 20 models, side view.
PDB entry 2l3l coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
The solution structure of the N-terminal domain of human tubulin binding cofactor C reveals a platform for tubulin interaction.
Garcia-Mayoral MF, Castaño R, Fanarraga ML, Zabala JC, Rico M, Bruix M
PLoS One 6 e25912 (2011)
PMID: 22028797

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172415 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tubulin-specific chaperone C Chain: A
Molecule details ›
Chain: A
Length: 111 amino acids
Theoretical weight: 13.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q15814 (Residues: 25-135; Coverage: 32%)
Gene name: TBCC
Sequence domains: Tubulin-specific chaperone C N-terminal domain
Structure domains: Tubulin Binding Cofactor C, N-terminal domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: molecular dynamics
Expression system: Escherichia coli

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Citations

5 citation in other articles

MicroRNA-1251-5p Promotes Carcinogenesis and Autophagy via Targeting the Tumor Suppressor TBCC in Ovarian Cancer Cells.
Shao et al. (2019)
4 more

4 mentions without citation

Tubulin-specific chaperones: components of a molecular machine that assembles the α/β heterodimer.
Tian et al. (2013)
3 more