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Solution NMR

SOLUTION NMR STRUCTURE OF THE GRB2 N-TERMINAL SH3 DOMAIN COMPLEXED WITH A TEN-RESIDUE PEPTIDE DERIVED FROM SOS DIRECT REFINEMENT AGAINST NOES, J-COUPLINGS, AND 1H AND 13C CHEMICAL SHIFTS, MINIMIZED AVERAGE STRUCTURE

Released:
DOI: 10.2210/pdb1gbq/pdb
PDB entry 1gbq coloured by chain, front view.
PDB entry 1gbq coloured by chain, side view.
PDB entry 1gbq coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Solution structure of the Grb2 N-terminal SH3 domain complexed with a ten-residue peptide derived from SOS: direct refinement against NOEs, J-couplings and 1H and 13C chemical shifts.
Wittekind M, Mapelli C, Lee V, Goldfarb V, Friedrichs MS, Meyers CA, Mueller L
J Mol Biol 267 933-52 (1997)
PMID: 9135122

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178798 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Growth factor receptor-bound protein 2 Chain: A
Molecule details ›
Chain: A
Length: 74 amino acids
Theoretical weight: 8.45 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q60631 (Residues: 1-61; Coverage: 28%)
Gene name: Grb2
Sequence domains: SH3 domain
Structure domains: SH3 Domains
Son of sevenless homolog 1 Chain: B
Molecule details ›
Chain: B
Length: 12 amino acids
Theoretical weight: 1.2 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
  • Canonical: Q62245 (Residues: 1135-1144; Coverage: 1%)
Gene name: Sos1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: DG, SA
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

3 review citations

Recognition of proline-rich motifs by protein-protein-interaction domains.
Ball et al. (2005)
2 more

8 mentions without citation

Peptide-based covalent inhibitors of protein-protein interactions.
Paulussen et al. (2023)
7 more