Crystal structure of human monoamine oxidase B, a drug target enzyme monotopically inserted into the mitochondrial outer membrane

Claudia Binda, Frantisek Hubálek, Min Li, Dale E. Edmondson, Andrea Mattevi

Research output: Contribution to journalArticlepeer-review

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 Å 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.

Original languageEnglish (US)
Pages (from-to)225-228
Number of pages4
JournalFEBS Letters
Volume564
Issue number3
DOIs
StatePublished - Apr 30 2004

Keywords

  • Flavin
  • Human monoamine oxidase B structure
  • MAO, monoamine oxidase
  • Mitochondrial membrane
  • Monotopic

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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