› 1ckb

X-ray diffraction
1.9Å resolution

STRUCTURAL BASIS FOR THE SPECIFIC INTERACTION OF LYSINE-CONTAINING PROLINE-RICH PEPTIDES WITH THE N-TERMINAL SH3 DOMAIN OF C-CRK

Released:
DOI: 10.2210/pdb1ckb/pdb
PDB entry 1ckb coloured by chain, front view.
PDB entry 1ckb coloured by chain, side view.
PDB entry 1ckb coloured by chain, top view.
Source organisms:
Primary publication:
Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk.
Wu X, Knudsen B, Feller SM, Zheng J, Sali A, Cowburn D, Hanafusa H, Kuriyan J
Structure 3 215-26 (1995)
PMID: 7735837

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-162136 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Adapter molecule crk Chain: A
Molecule details ›
Chain: A
Length: 57 amino acids
Theoretical weight: 6.81 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q64010 (Residues: 134-190; Coverage: 19%)
Gene names: Crk, Crko
Sequence domains: SH3 domain
Structure domains: SH3 Domains
SOS PEPTIDE (PRO-PRO-PRO-VAL-PRO-PRO-ARG-ARG-ARG-ARG) Chain: B
Molecule details ›
Chain: B
Length: 10 amino acids
Theoretical weight: 1.23 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P41
Unit cell:
a: 47.4Å b: 47.4Å c: 29.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.183 not available
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

20 review citations

Crk family adaptors-signalling complex formation and biological roles.
Feller SM. (2001)
19 more

16 mentions without citation

Specificity and versatility of SH3 and other proline-recognition domains: structural basis and implications for cellular signal transduction.
Li SS. (2005)
15 more