Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
