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Solution NMR

Structure of the hDLG/SAP97 PDZ2 in complex with HPV-18 papillomavirus E6 peptide

Released:
DOI: 10.2210/pdb2oqs/pdb
PDB entry 2oqs coloured by chain, ensemble of 30 models, front view.
PDB entry 2oqs coloured by chain, ensemble of 30 models, side view.
PDB entry 2oqs coloured by chain, ensemble of 30 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the hDlg/SAP97 PDZ2 domain and its mechanism of interaction with HPV-18 papillomavirus E6 protein.
Liu Y, Henry GD, Hegde RS, Baleja JD
Biochemistry 46 10864-74 (2007)
PMID: 17713926

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163125 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Disks large homolog 1 Chain: A
Molecule details ›
Chain: A
Length: 97 amino acids
Theoretical weight: 10.4 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q12959 (Residues: 318-406; Coverage: 10%)
Gene name: DLG1
Sequence domains: PDZ domain
Structure domains: Pdz3 Domain
C-terminal HPV-18 E6 peptide Chain: B
Molecule details ›
Chain: B
Length: 6 amino acids
Theoretical weight: 790 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

7 review citations

The emerging contribution of sequence context to the specificity of protein interactions mediated by PDZ domains.
Luck et al. (2012)
6 more

6 mentions without citation

Specificity in PDZ-peptide interaction networks: Computational analysis and review.
Amacher et al. (2020)
5 more