Structure of human monoamine oxidase A at 2.2-Å resolution: The control of opening the entry for substrates/inhibitors

Proceedings of the National Academy of Sciences of the United States of America

Volumn 105, Issue 15, 2008, Pages 5739-5744

  Son, Se Young ^a   Ma, Jichun ^b   Kondou, Youhei ^c   Yoshimura, Masato ^a   Yamashita, Eiki ^a   Tsukihara, Tomitake ^a  

^a OSAKA UNIVERSITY   (Japan)

^b NATIONAL CANCER INSTITUTE   (United States)

^c KOBE UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

Author keywords

Harmine; Single transmembrane helix; Transmembrane helical anchor; X ray structure

Indexed keywords

AMINE OXIDASE (FLAVIN CONTAINING) ISOENZYME A; AMINE OXIDASE (FLAVIN CONTAINING) ISOENZYME B; AMINO ACID DERIVATIVE; MUTANT PROTEIN; TYROSINE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; COMPARATIVE STUDY; CONTROLLED STUDY; ELECTRON; ENZYME ACTIVITY; ENZYME STRUCTURE; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; WILD TYPE;

BINDING SITES; CRYSTALLOGRAPHY, X-RAY; HUMANS; MONOAMINE OXIDASE; MONOAMINE OXIDASE INHIBITORS; POINT MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY;

RATTUS;

EID: 44449117421     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0710626105     Document Type: Article

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