Crystallization and preliminary crystallographic analysis of rat monoamine oxidase A complexed with clorgyline

Authors: Ma, Jichun; Kubota, Fumie; Yoshimura, Masato; Yamashita, Eiki; Nakagawa, Atsushi; Ito, Akio; Tsukihara, Tomitake

Source: Acta Crystallographica Section D, Volume 60, Number 2, 1 February 2004 , pp. 317-319(3)

Publisher: Blackwell Publishing

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Abstract:

Monoamine oxidase (MAO) is an FAD-containing mitochondrial outer-membrane protein which catalyzes the degradation of several neurotransmitters in the central nervous system. The two subtypes of MAO, MAOA and MAOB, have similar primary sequences but different substrate and inhibitor specificities. The structure of human MAOB has recently been determined, but the structure of MAOA remains unknown. To clarify the mechanisms underlying their unique substrate and inhibitor recognition and thereby facilitate the development of new specific inhibitors to treat MAO-related neurological disorders, rat MAOA was crystallized in a complex with the specific inhibitor clorgyline. Diffraction data were collected to 3.2 Å resolution. The crystal belongs to the space group P4₃2₁2, with unit-cell parameters a = b = 158.2, c = 258.4 Å.

Keywords: monoamine oxidase; membrane proteins

Document Type: Research article

DOI: 10.1107/S0907444903025770

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