Structure of the unliganded form of the proprotein convertase furin suggests activation by a substrate-induced mechanism

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

Volumn 113, Issue 40, 2016, Pages 11196-11201

  Dahms, Sven O ^a,h   Arciniega, Marcelino ^b   Steinmetzer, Torsten ^c   Huber, Robert ^d,e,f,g   Than, Manuel E ^a  

^a FRITZ LIPMANN INSTITUTE   (Germany)

^b INSTITUTO DE FISIOLOGÍA CELULAR   (Mexico)

^c PHILIPPS UNIVERSITY MARBURG   (Germany)

^d MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^e TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^f UNIVERSITY OF DUISBURG ESSEN   (Germany)

^g CARDIFF UNIVERSITY   (United Kingdom)

^h UNIVERSITY OF SALZBURG   (Austria)

Author keywords

Activation; Conformational transition; Serine protease; Specificity

Indexed keywords

FURIN; PROPROTEIN CONVERTASE 1; CALCIUM; LIGAND;

ARTICLE; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; HUMAN; MOLECULAR DYNAMICS; MOLECULAR RECOGNITION; PRIORITY JOURNAL; ANTAGONISTS AND INHIBITORS; CHEMISTRY; METABOLISM; PRINCIPAL COMPONENT ANALYSIS; PROTEIN CONFORMATION; STATIC ELECTRICITY; STRUCTURAL HOMOLOGY; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

CALCIUM; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; FURIN; HUMANS; LIGANDS; MOLECULAR DYNAMICS SIMULATION; PRINCIPAL COMPONENT ANALYSIS; PROTEIN CONFORMATION; STATIC ELECTRICITY; STRUCTURAL HOMOLOGY, PROTEIN; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 84989950483     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1613630113     Document Type: Article

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