› 2l2p

Solution NMR

Folding Intermediate of the Fyn SH3 A39V/N53P/V55L from NMR Relaxation Dispersion Experiments

Released:
DOI: 10.2210/pdb2l2p/pdb
PDB entry 2l2p coloured by chain, ensemble of 10 models, front view.
PDB entry 2l2p coloured by chain, ensemble of 10 models, side view.
PDB entry 2l2p coloured by chain, ensemble of 10 models, top view.
Source organism: Gallus gallus
Primary publication:
Structure of an intermediate state in protein folding and aggregation.
Neudecker P, Robustelli P, Cavalli A, Walsh P, Lundström P, Zarrine-Afsar A, Sharpe S, Vendruscolo M, Kay LE
Science 336 362-6 (2012)
PMID: 22517863

Function and Biology Details

Reaction catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170261 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase Fyn Chain: A
Molecule details ›
Chain: A
Length: 66 amino acids
Theoretical weight: 7.54 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q05876 (Residues: 85-142; Coverage: 11%)
Gene name: FYN
Sequence domains: SH3 domain
Structure domains: SH3 Domains

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 73%
Refinement method: molecular dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

36 review citations

The amyloid state and its association with protein misfolding diseases.
Knowles et al. (2014)
35 more

3 mentions without citation

NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers.
Sekhar et al. (2013)
2 more