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Publication Abstract from PubMed

HIV-1 integrase (HIV-1 IN) is an enzyme produced by the HIV-1 virus that integrates genetic material of the virus into the DNA of infected human cells. HIV-1 IN acts as a key component of the Retroviral Pre-Integration Complex (PIC). Protein dynamics could play an important role during the catalysis of HIV-1 IN; however, this process has not yet been fully elucidated. X-ray free electron laser (XFEL) together with nuclear magnetic resonance (NMR) could provide information regarding the dynamics during this catalysis reaction. Here, we report the non-cryogenic crystal structure of HIV-1 IN catalytic core domain at 2.5 A using microcrystals in XFELs. Compared to the cryogenic structure at 2.1 A using conventional synchrotron crystallography, there was a good agreement between the two structures, except for a catalytic triad formed by Asp64, Asp116, and Glu152 (DDE) and the lens epithelium-derived growth factor binding sites. The helix III region of the 140-153 residues near the active site and the DDE triad show a higher dynamic profile in the non-cryogenic structure, which is comparable to dynamics data obtained from NMR spectroscopy in solution state.

Non-Cryogenic Structure and Dynamics of HIV-1 Integrase Catalytic Core Domain by X-ray Free-Electron Lasers.,Park JH, Yun JH, Shi Y, Han J, Li X, Jin Z, Kim T, Park J, Park S, Liu H, Lee W Int J Mol Sci. 2019 Apr 20;20(8). pii: ijms20081943. doi: 10.3390/ijms20081943. PMID:31010024^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.