-
Views
-
Cite
Cite
Yusuke Nomura, Takao Masuda, Gota Kawai, Structural Analysis of a Mutant of the HIV-1 Integrase Zinc Finger Domain That Forms a Single Conformation, The Journal of Biochemistry, Volume 139, Issue 4, April 2006, Pages 753–759, https://doi.org/10.1093/jb/mvj085
Close - Share Icon Share
Abstract
HIV-1 integrase consists of three functional domains, an N-terminal zinc finger domain, a catalytic core domain and a C-terminal DNA binding domain. NMR analysis of an isolated N-terminal domain (IN1–55) has shown that IN1–55 exists in two conformational states [E and D forms; Cai et al. (1997) Nat. Struct. Biol. 4, 567–577]. The two forms differ in the coordination of the zinc ion by two histidine residues. In the present study, structural analysis of a mutant of IN1–55, Y15A, by NMR spectroscopy indicated that the mutant protein folds correctly but takes only the E form. Since the Y15A mutation abrogates the HIV-1 infectivity, Y15 might have some important role in the full-length integrase activity during the virus infection cycle. Our results suggest a possible role of Y15 in structural transition between the E and D forms of HIV-1 integrase to allow the optimal tetramerization.
