3avj

X-ray diffraction
1.7Å resolution

Crystal structures of novel allosteric peptide inhibitors of HIV integrase in the LEDGF binding site

Released:

Function and Biology Details

Reactions catalysed:
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid
Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.
Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-536893 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Integrase Chains: A, B
Molecule details ›
Chains: A, B
Length: 183 amino acids
Theoretical weight: 20.04 KDa
Source organism: Human immunodeficiency virus type 1 (NEW YORK-5 ISOLATE)
Expression system: Escherichia coli
UniProt:
  • Canonical: P12497 (Residues: 1197-1359; Coverage: 11%)
Gene name: gag-pol
Sequence domains: Integrase core domain
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H
LEDGF peptide Chains: D, F
Molecule details ›
Chains: D, F
Length: 8 amino acids
Theoretical weight: 920 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P31
Unit cell:
a: 71.015Å b: 71.015Å c: 67.018Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.159 0.158 0.198
Expression systems:
  • Escherichia coli
  • Not provided