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Structure of a two‐domain fragment of HIV‐1 integrase: implications for domain organization in the intact protein
Author(s) -
Wang JianYong,
Ling Hong,
Yang Wei,
Craigie Robert
Publication year - 2001
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/20.24.7333
Subject(s) - integrase , biology , tetramer , dimer , protein structure , transposase , dna , genetics , enzyme , biochemistry , gene , genome , physics , transposable element , nuclear magnetic resonance
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, Tn 5 , and exhibits positively charged channels suitable for DNA binding.