Lysine 156 promotes the anomalous proenzyme activity of tPA: X-ray crystal structure of single-chain human tPA

EMBO Journal

Volumn 16, Issue 16, 1997, Pages 4797-4805

  Renatus, Martin ^a   Engh, Richard A ^a,b   Stubbs, Milton T ^a,c   Huber, Robert ^a   Fischer, Stephan ^b   Kohnert, Ulrich ^b   Bode, Wolfram ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^b F HOFFMANN LA ROCHE LTD   (Switzerland)

^c PHILIPPS UNIVERSITY MARBURG   (Germany)

Author keywords

Activation; Crystal structure; Fibrinolysis; Plasminogen activator; Zymogen

Indexed keywords

BLOOD CLOTTING FACTOR 10A; FIBRIN; LYSINE; PLASMIN; RECOMBINANT PROTEIN; SERINE PROTEINASE; TISSUE PLASMINOGEN ACTIVATOR; TRYPSIN; UROKINASE;

ACUTE HEART INFARCTION; ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DRUG DESIGN; ENZYME ACTIVITY; FIBRINOLYSIS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN STRUCTURE; X RAY CRYSTALLOGRAPHY;

AMINO ACID CHLOROMETHYL KETONES; ASPARTIC ACID; BINDING SITES; CHYMOTRYPSINOGEN; CRYSTALLOGRAPHY, X-RAY; DANSYL COMPOUNDS; ENZYME ACTIVATION; ESCHERICHIA COLI; FLUORESCENT DYES; HUMANS; LYSINE; MODELS, MOLECULAR; PLASMINOGEN ACTIVATORS; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SERINE ENDOPEPTIDASES; SERINE PROTEINASE INHIBITORS; TISSUE PLASMINOGEN ACTIVATOR;

EID: 0030742394     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.16.4797     Document Type: Article

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