The structure of bovine lysosomal α-mannosidase suggests a novel mechanism for low-pH activation

Journal of Molecular Biology

Volumn 327, Issue 3, 2003, Pages 631-644

  Heikinheimo, Pirkko ^a   Helland, Ronny ^a   Leiros, Hanna Kirsti Schrøder ^a   Leiros, Ingar ^a   Karlsen, Solveig ^a,e   Evjen, Gry ^a   Ravelli, Raimond ^b   Schoehn, Guy ^b,c   Ruigrok, Rob ^b   Tollersrud, Ole Kristian ^a   McSweeney, Seán ^b,d   Hough, Edward ^a  

^a UNIVERSITY OF TROMSØ   (Norway)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (France)

^c INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^d EUROPEAN SYNCHROTRON RADIATION FACILITY   (France)

^e UNIVERSITY OF OSLO   (Norway)

Author keywords

Crystal structure; Glycoside hydrolase; Lysosomal; Mannosidosis; mannosidase

Indexed keywords

ALPHA MANNOSIDASE; DIMER; GLYCOSIDASE; GLYCOSIDE HYDROLASE 38; ISOENZYME; MANNOSE; UNCLASSIFIED DRUG;

ACIDITY; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; ELECTRON MICROSCOPY; ENZYME ACTIVATION; ENZYME MECHANISM; ENZYME STRUCTURE; GENE MUTATION; INTRACELLULAR TRANSPORT; LYSOSOME; MANNOSIDOSIS; NONHUMAN; PH; PHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN DATABASE; PROTEIN FAMILY;

BOS TAURUS; BOVINAE; CAVIA PORCELLUS; FELIS CATUS; MAMMALIA; SUS SCROFA;

EID: 0037470630     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00172-4     Document Type: Article

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