Abstract:
:Monoamine oxidase B (MAO B) is an outer mitochondrial membrane protein that oxidizes arylalkylamine neurotransmitters and has been a valuable drug target for many neurological disorders. The 1.7 angstrom resolution structure of human MAO B shows the enzyme is dimeric with a C-terminal transmembrane helix protruding from each monomer and anchoring the protein to the membrane. This helix departs perpendicularly from the base of the structure in a different way with respect to other monotopic membrane proteins. Several apolar loops exposed on the protein surface are located in proximity of the C-terminal helix, providing additional membrane-binding interactions. One of these loops (residues 99-112) also functions in opening and closing the MAO B active site cavity, which suggests that the membrane may have a role in controlling substrate binding.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Binda C,Hubálek F,Li M,Edmondson DE,Mattevi Adoi
10.1016/S0014-5793(04)00209-1keywords:
subject
Has Abstractpub_date
2004-04-30 00:00:00pages
225-8issue
3eissn
0014-5793issn
1873-3468pii
S0014579304002091journal_volume
564pub_type
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