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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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Fatty acid amide hydrolase (FAAH) is a member of the amidase signature (AS) family of serine hydrolases. FAAH hydrolyzesanandamide and oleamide, which regulate pain perception, inflammation, and the cognitive state. Thus far, a limitednumber of structures of mammalian FAAH and non-mammalian AS family members have been determined. In this study,to understand structural features and functional diversity of FAAH, we crystallized the FAAH protein from the pathogenicfungus Candida albicans. X-ray diffraction data were obtained at 2.2 Å resolution. The crystal of the C. albicans FAAH(CaFAAH) belonged to P21, with the unit cell parameters a = 84.8, b = 68.7, c = 100.9 Å, α = γ = 90, and β = 99.6°. Thecrystals contained two CaFAAH molecules in asymmetric units.
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참고문헌 (16)
참고문헌 신청
Adams, P. D. / 2010 / PHENIX : a comprehensive Python-based system for macromolecular structure solution / Acta Crystallogr D Biol Crystallogr 66:213~221
Ahn, K. / 2008 / Enzymatic pathways that regulate endocannabinoid signaling in the nervous system / Chemical reviews 108:1687~1707
Bertolacci, L. / 2013 / A binding site for nonsteroidal anti-inflammatory drugs in fatty acid amide hydrolase / J Am Chem Soc 135:22~25
Blaise, M. / 2010 / Crystal structure of a transfer-ribonucleoprotein particle that promotes asparagine formation / EMBO J 29:3118~3129
Bracey, M. H. / 2002 / Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling / Science 298:1793~1796
Ahn, K. / 2008 / Enzymatic pathways that regulate endocannabinoid signaling in the nervous system / Chemical reviews 108:1687~1707
Bertolacci, L. / 2013 / A binding site for nonsteroidal anti-inflammatory drugs in fatty acid amide hydrolase / J Am Chem Soc 135:22~25
Blaise, M. / 2010 / Crystal structure of a transfer-ribonucleoprotein particle that promotes asparagine formation / EMBO J 29:3118~3129
Bracey, M. H. / 2002 / Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling / Science 298:1793~1796
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