GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
PMID:9735293
| Citation |
Maignan, S, Guilloteau, JP, Zhou-Liu, Q, Clément-Mella, C and Mikol, V (1998) 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. 282:359-68 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1006/jmbi.1998.2002 |
| Keywords |
Binding Sites; Cacodylic Acid/metabolism; Catalysis; Crystallography, X-Ray; HIV Integrase/chemistry; HIV Integrase/metabolism; Magnesium/chemistry; Magnesium/metabolism; Models, Chemical; Molecular Structure; Protein Structure, Tertiary |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
|
enables |
GO:0000287: magnesium ion binding |
ECO:0000315: mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0042803: protein homodimerization activity |
ECO:0000315: mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
Notes
See also
References
See Help:References for how to manage references in GONUTS.
