有哪些信誉好的足球投注网站defining the functional domain of programmed cell death 10 through its interactions with phosphatidylinositol-3,4,5-trisphosphate定义的功能域程序性细胞死亡10与phosphatidylinositol-3交互,4,5-trisphosphate.pdfVIP
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defining the functional domain of programmed cell death 10 through its interactions with phosphatidylinositol-3,4,5-trisphosphate定义的功能域程序性细胞死亡10与phosphatidylinositol-3交互,4,5-trisphosphate
Defining the Functional Domain of Programmed Cell Death 10 through Its Interactions with Phosphatidylinositol-3,4,5-Trisphosphate 1 3 1 2 1 Christopher F. Dibble , Jeremy A. Horst , Michael H. Malone , Kun Park , Brenda Temple , Holly 2 2 1 1,2 Cheeseman , Justin R. Barbaro , Gary L. Johnson , Sompop Bencharit * 1 Department of Pharmacology, School of Medicine, and the Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, North Carolina, United States of America, 2 Department of Prosthodontics and the Dental Research Center, School of Dentistry, University of North Carolina, Chapel Hill, North Carolina, United States of America, 3 Department of Microbiology, School of Medicine, and Department of Oral Biology, School of Dentistry, University of Washington, Seattle, Washington, United States of America Abstract Cerebral cavernous malformations (CCM) are vascular abnormalities of the central nervous system predisposing blood vessels to leakage, leading to hemorrhagic stroke. Three genes, Krit1 (CCM1), OSM (CCM2), and PDCD10 (CCM3) are involved in CCM development. PDCD10 binds specifically to PtdIns(3,4,5)P3 and OSM. Using threading analysis and multi-template modeling, we constructed a three-dimensional model of PDCD10. PDCD10 appears to be a six-helical-bundle protein formed by two heptad-repeat-hairpin structures (a1–3 and a4–6) sharing the closest 3D homology with the bacterial phosphate transporter, PhoU. We identified a stretch of five lysines forming an amphipathic helix, a potential PtdIns(3,4,5)P3 binding site, in the a5 helix. We generated a recombinant wild
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