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Solution NMR

SOLUTION STRUCTURE OF THE ENA-VASP HOMOLOGY 1 (EVH1) DOMAIN OF HUMAN VASODILATOR-STIMULATED PHOSPHOPROTEIN (VASP)

Released:
DOI: 10.2210/pdb1egx/pdb
PDB entry 1egx coloured by chain, ensemble of 15 models, front view.
PDB entry 1egx coloured by chain, ensemble of 15 models, side view.
PDB entry 1egx coloured by chain, ensemble of 15 models, top view.
Source organism: Homo sapiens
Primary publication:
Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity.
Ball LJ, Kühne R, Hoffmann B, Häfner A, Schmieder P, Volkmer-Engert R, Hof M, Wahl M, Schneider-Mergener J, Walter U, Oschkinat H, Jarchau T
EMBO J 19 4903-14 (2000)
PMID: 10990454

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156222 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vasodilator-stimulated phosphoprotein Chain: A
Molecule details ›
Chain: A
Length: 115 amino acids
Theoretical weight: 12.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P50552 (Residues: 1-115; Coverage: 30%)
Gene name: VASP
Sequence domains: WH1 domain
Structure domains: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing torsion angle dynamics
Expression system: Escherichia coli BL21

Quick links

Citations

15 review citations

Ena/VASP proteins: regulators of the actin cytoskeleton and cell migration.
Krause et al. (2003)
14 more

5 mentions without citation

Diversity of polyproline recognition by EVH1 domains.
Peterson et al. (2009)
4 more