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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.

SUBMITTER: Wang JY

PROVIDER: S-EPMC125787 | biostudies-literature | 2001 Dec

REPOSITORIES: biostudies-literature

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Structure of a two-domain fragment of HIV-1 integrase: implications for domain organization in the intact protein.

Wang J Y JY Ling H H Yang W W Craigie R R

The EMBO journal 20011201 24

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 fo ...[more]

PMID: 11743009

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