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Report No.
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Structure determination of perdeuterated human immunodeficiency virus type 1 protease (HIV-1PR)

Honjo, Eijiro; Adachi, Motoyasu; Tamada, Taro; Kuroki, Ryota

Because human immunodeficiency virus type 1 protease (HIV-1PR, 99 amino acids) is involved in the maturation of HIV-1, it is a prime target for antiviral therapy of AIDS. In order to investigate precise structure-function relationship, we are planning to determine the structure of HIV-1PR including the information of hydrogen and hydrating water molecules using high resolution X-ray crystallography and neutron crystallography. For higher resolution neutron protein crystallography, it is necessary to exchange hydrogen (H) atoms with deuterium (D) atoms in order to reduce background noise derived from incoherent neutron scattering cross-section of hydrogen. Therefore, we have expressed fully deuterated HIV-1PR using commercially available perdeuterated medium. X-ray structures of non labeled and perdeuterated HIV-1PR were determined to 1.2 and 1.4${AA}$ resolution, respectively, using crystals grown under the same conditions. Both structures did not show any significant changes.

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