New general approach for determining the solution structure of a ligand bound weakly to a receptor: Structure of a fibrinogen Aα-like peptide bound to thrombin(S195A) obtained using NOE distance constraints and an ECEPP/3 flexible docking program

Proteins: Structure, Function and Genetics

Volumn 34, Issue 1, 1999, Pages 29-48

  Maurer, Muriel C ^a,b   Trosset, Jean Yves ^a   Lester, Cathy C ^a   DiBella, Elsie E ^a,c   Scheraga, Harold A ^a  

^a Department of Obstetrics Gynecology   (United States)

^b UNIVERSITY OF LOUISVILLE   (United States)

^c BRISTOL MYERS SQUIBB   (United States)

Author keywords

Fibrinogen A ; Flexible docking; MR; Thrombin

Indexed keywords

FIBRINOGEN; LIGAND; MUTANT PROTEIN; PROLINE; RECEPTOR; THROMBIN;

ARTICLE; CONFORMATION; ENZYME ACTIVE SITE; LIGAND BINDING; MOLECULAR INTERACTION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; SIMULATION;

ANIMALS; BINDING SITES; CATTLE; CIRCULAR DICHROISM; COMPUTER SIMULATION; ESCHERICHIA COLI; FIBRINOGEN; KINETICS; LIGANDS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, CHEMICAL; MODELS, MOLECULAR; MONTE CARLO METHOD; PLASMIDS; POINT MUTATION; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; THROMBIN;

EID: 0032910684     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19990101)34:1<29::AID-PROT4>3.0.CO;2-U     Document Type: Article

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