1k6y
From Proteopedia
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Crystal Structure of a Two-Domain Fragment of HIV-1 Integrase
Overview
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.
About this Structure
1K6Y is a Single protein structure of sequence from Human immunodeficiency virus 1 with ZN, K and PO4 as ligands. Active as RNA-directed DNA polymerase, with EC number 2.7.7.49 Full crystallographic information is available from OCA.
Reference
Structure of a two-domain fragment of HIV-1 integrase: implications for domain organization in the intact protein., Wang JY, Ling H, Yang W, Craigie R, EMBO J. 2001 Dec 17;20(24):7333-43. PMID:11743009
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