Refined solution structure of the dimeric N-terminal HHCC domain of HIV-2 integrase |
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Authors: | Astrid P.A.M. Eijkelenboom Fusinita M.I. van den Ent Rainer Wechselberger Ronald H.A. Plasterk Robert Kaptein Rolf Boelens |
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Affiliation: | (1) Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands;(2) Division of Molecular Biology, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands |
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Abstract: | The solution structure of the dimeric N-terminal domain of HIV-2 integrase (residues 1–55, named IN1–55) has been determined using NMR spectroscopy. The structure of the monomer, which was already reported previously [Eijkelenboom et al. (1997) Curr. Biol., 7, 739–746], consists of four -helices and is well defined. Helices 1, 2 and 3 form a three-helix bundle that is stabilized by zinc binding to His12, His16, Cys40 and Cys43. The dimer interface is formed by the N-terminal tail and the first half of helix 3. The orientation of the two monomeric units with respect to each other shows considerable variation. 15N relaxation studies have been used to characterize the nature of the intermonomeric disorder. Comparison of the dimer interface with that of the well-defined dimer interface of HIV-1 IN1–55 shows that the latter is stabilized by additional hydrophobic interactions and a potential salt bridge. Similar interactions cannot be formed in HIV-2 IN1–55 [Cai et al. (1997) Nat. Struct. Biol., 4, 567–577], where the corresponding residues are positively charged and neutral ones. |
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Keywords: | helix-turn-helix motif HIV integrase protein dimer protein structure zinc-binding domain |
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