title: Structure of a two-domain fragment of HIV-1 integrase: implications for domain organization in the intact protein.
abstract: Retroviral integrase, an essential enzyme for replication of human immunodeficiency virus type-1 (HIV-1) and other retroviruses, contains three structurally distinct domains, an N-terminal domain, the catalytic core and a C-terminal domain. To elucidate their spatial arrangement, we have solved the structure of a fragment of HIV-1 integrase comprising the N-terminal and catalytic core domains. This structure reveals a dimer interface between the N-terminal domains different from that observed for the isolated domain. It also complements the previously determined structure of the C-terminal two domains of HIV-1 integrase; superposition of the conserved catalytic core of the two structures results in a plausible full-length integrase dimer. Furthermore, an integrase tetramer formed by crystal lattice contacts bears structural resemblance to a related bacterial transposase, Tn5, and exhibits positively charged channels suitable for DNA binding.
authors.affiliation: Laboratory of Molecular Biology, NIDDK, National Institutes of Health, 5 Center Drive MSC 0560, Bethesda, MD 20892, USA.
authors.forename: J Y
authors.initials: JY
authors.lastname: Wang
authors.forename: H
authors.initials: H
authors.lastname: Ling
authors.forename: W
authors.initials: W
authors.lastname: Yang
authors.forename: R
authors.initials: R
authors.lastname: Craigie
mesh_terms: D020134:Catalytic Domain; D019427:HIV Integrase / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D010446:Peptide Fragments; D019427:HIV Integrase