Ligand preferences of kringle 2 and homologous domains of human plasminogen: Canvassing weak, intermediate, and high-affinity binding sites by 1H-NMR

Biochemistry

Volumn 36, Issue 39, 1997, Pages 11591-11604

  Marti, Daniel N ^a   Hu, Chih Kao ^a   An, Seong Soo A ^a   Von Haller, Priska ^b   Schaller, Johann ^b   Llinás, Miguel ^a  

^a CARNEGIE MELLON UNIVERSITY   (United States)

^b UNIVERSITY OF BERN   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

PLASMINOGEN;

ARTICLE; BINDING AFFINITY; BINDING SITE; ENZYME ANALYSIS; ENZYME BINDING; ENZYME CONFORMATION; EQUILIBRIUM CONSTANT; HUMAN; KRINGLE DOMAIN; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BINDING SITES; HUMANS; KRINGLES; LIGANDS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PLASMINOGEN; PROTEIN BINDING; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT;

EID: 0030852456     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi971316v     Document Type: Article

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