1BHL

CACODYLATED CATALYTIC DOMAIN OF HIV-1 INTEGRASE

Summary for 1BHL

• Entry DOI: 10.2210/pdb1bhl/pdb
• Descriptor: HIV-1 INTEGRASE (2 entities in total)
• Functional Keywords: dna integration, aids, polyprotein, hydrolase, endonuclease, polynucleotidyl transferase, dna binding (viral)
• Biological source: Human immunodeficiency virus 1
• Cellular location: Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P12497
• Total number of polymer chains: 1
• Total formula weight: 16756.84

Authors

Maignan, S.,Guilloteau, J.P.,Zhou-Liu, Q.,Clement-Mella, C.,Mikol, V. (deposition date: 1998-06-10, release date: 1998-10-14, Last modification date: 2024-11-20)

Primary citation

Maignan, S.,Guilloteau, J.P.,Zhou-Liu, Q.,Clement-Mella, C.,Mikol, V.
Crystal structures of the catalytic domain of HIV-1 integrase free and complexed with its metal cofactor: high level of similarity of the active site with other viral integrases.
J.Mol.Biol., 282:359-368, 1998

PubMed Abstract: Human immunodeficiency virus (HIV) integrase is the enzyme responsible for insertion of a DNA copy of the viral genome into host DNA, an essential step in the replication cycle of HIV. HIV-1 integrase comprises three functional and structural domains: an N-terminal zinc-binding domain, a catalytic core domain and a C-terminal DNA-binding domain. The catalytic core domain with the F185H mutation has been crystallized without sodium cacodylate in a new crystal form, free and complexed with the catalytic metal Mg2+. The structures have been determined and refined to about 2.2 A. Unlike the previously reported structures, the three active-site carboxylate residues (D,D-35-E motif) are well ordered and both aspartate residues delineate a proper metal-binding site. Comparison of the active binding site of this domain with that of other members from the polynucleotidyl transferases superfamily shows a high level of similarity, providing a confident template for the design of antiviral agents.

PubMed: 9735293
DOI: 10.1006/jmbi.1998.2002

Experimental method

X-RAY DIFFRACTION (2.2 Å)