DNA nucleotidyltransferase (RNA-directed)
RNA-dependent deoxyribonucleate nucleotidyltransferase
desoxyuridine 5'-triphosphate nucleotidohydrolase
ACE-ALN-VAL-LEU-ALA-GLU-ALN-NH2 (chain I, J)
This enzyme is composed of retropepsin (EC 3.4.23.-), RNA-directed DNA polymerase (EC 2.7.7.49), RNase H (EC 3.1.26.4), dUTP pyrophosphatase (EC 3.6.1.23), and integrase. The tertiary structures have been solved only for retropepsin (EC 3.4.23.-) and dUTP pyrophosphatase (EC 3.6.1.23). The dUTP pyrophosphatase domain (EC 3.6.1.23) forms a trimer, which binds one Mg2+ ion (see PDB;1dut). The domains which corresponds to protease domain (EC 3.4.23.-) belong to the peptidase family-A2. Although this domain has a catalytic aspartic residue, it forms a homodimer with a single active site with a typical catalytic dyad, composed of two aspartic acid residues. According to the literature [4], the catalytic mechanism is very similar to that of pepsin (see D00436 in EzCatDB).
Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A
HIV Type 1 Reverse Transcriptase; Chain A, domain 1
Structure of an inhibitor complex of the proteinase from feline immunodeficiency virus.
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 42-154. Retropepsin (3.4.23.-)
Structures of feline immunodeficiency virus dUTP pyrophosphatase and its nucleotide complexes in three crystal forms.
Design, synthesis, and biological evaluation of HIV/FIV protease inhibitors incorporating a conformationally constrained macrocycle with a small P3' residue.
Structural basis for distinctions between substrate and inhibitor specificities for feline immunodeficiency virus and human immunodeficiency virus proteases.
Inhibitor design by wrapping packing defects in HIV-1 proteins.
The monomeric dUTPase from Epstein-Barr virus mimics trimeric dUTPases.
C2-symmetrical tetrahydroxyazepanes as inhibitors of glycosidases and HIV/FIV proteases.
Crystal structure of dUTP pyrophosphatase from feline immunodeficiency virus.
Crystal structures of the inactive D30N mutant of feline immunodeficiency virus protease complexed with a substrate and an inhibitor.
Toward a universal inhibitor of retroviral proteases: comparative analysis of the interactions of LP-130 complexed with proteases from HIV-1, FIV, and EIAV.
X-ray crystallography. Retropepsin (3.4.23.-)
Comparison of inhibitor binding to feline and human immunodeficiency virus proteases: structure-based drug design and the resistance problem.
Methodology for protein-ligand binding studies: application to a model for drug resistance, the HIV/FIV protease system.
Structure/function analysis of a dUTPase: catalytic mechanism of a potential chemotherapeutic target.
Structural studies of FIV and HIV-1 proteases complexed with an efficient inhibitor of FIV protease.