1mfs

Solution NMR

DYNAMICAL BEHAVIOR OF THE HIV-1 NUCLEOCAPSID PROTEIN; NMR, 30 STRUCTURES

Released:
Source organism: Human immunodeficiency virus
Primary publication:
Dynamical behavior of the HIV-1 nucleocapsid protein.
J Mol Biol 279 633-49 (1998)
PMID: 9641983

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:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-153078 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nucleocapsid protein p7 Chain: A
Molecule details ›
Chain: A
Length: 55 amino acids
Theoretical weight: 6.39 KDa
Source organism: Human immunodeficiency virus
Expression system: Escherichia coli
UniProt:
  • Canonical: P35963 (Residues: 378-432; Coverage: 4%)
Gene name: gag-pol
Sequence domains: Zinc knuckle
Structure domains: Zinc finger, CCHC-type

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry
Expression system: Escherichia coli