Latency and substrate binding globally reduce solvent accessibility of Plasminogen Activator Inhibitor type 1 (PAI-1): An adaptation of PAI-1 conformer crystal structures by hydrogen-deuterium exchange

Journal of Biological Chemistry

Volumn 279, Issue 48, 2004, Pages 50132-50141

  Nukuna, Benedicta N ^a,c   Penn, Marc S ^a   Anderson, Vernon E ^b   Hazen, Stanley L ^a,d  

^a CASE WESTERN RESERVE UNIVERSITY   (United States)

^b CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c ASTRAZENECA   (United Kingdom)

^d LERNER RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANNEALING; CATALYST ACTIVITY; COMPUTER SIMULATION; DEUTERIUM; HYDROGEN; MAPPING; MASS SPECTROMETRY; PROTEINS; X RAY CRYSTALLOGRAPHY;

CELL MIGRATION; SUBSTRATE BINDING; TISSUE REMODELING;

CELLS;

AMIDE; DEUTERIUM; HYDROGEN; PEPTIDE; PLASMINOGEN ACTIVATOR INHIBITOR 1; SOLVENT;

ARTICLE; BINDING AFFINITY; CONFORMATION; EXPOSURE; HUMAN; MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PLASMINOGEN ACTIVATOR INHIBITOR 1; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SOLVENTS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; SUBSTRATE SPECIFICITY;

EID: 9644273956     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M407548200     Document Type: Article

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