Ligand interactions with the kringle 5 domain of plasminogen. A study by 1H NMR spectroscopy.
Open Access
- 1 March 1990
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 265 (7), 3906-3915
- https://doi.org/10.1016/s0021-9258(19)39679-6
Abstract
No abstract availableThis publication has 36 references indexed in Scilit:
- α2-antiplasmin's carboxy-terminal lysine residue is a major site of interaction with plasminBiochemical and Biophysical Research Communications, 1988
- Structure of prothrombin fragment 1 refined at 2.8 Å resolutionJournal of Molecular Biology, 1988
- Binding site of α2-plasmin inhibitor to plasminogenBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988
- Proton magnetic resonance study of lysine-binding to the kringle 4 domain of human plasminogenJournal of Molecular Biology, 1987
- Complete assignment of the aromatic proton magnetic resonance spectrum of the kringle 1 domain from human plasminogen: the structure of the ligand-binding siteBiochemistry, 1987
- Isolation, purification and 1H-NMR characterization of a kringle 5 domain fragment from human plasminogenBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1987
- Proton Overhauser experiments on kringle 4 from human plasminogen. Implications for the structure of the kringles' hydrophobic coreBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985
- CHARMM: A program for macromolecular energy, minimization, and dynamics calculationsJournal of Computational Chemistry, 1983
- Kringle 5 of human plasminogen carries a benzamidine-binding siteBiochemical and Biophysical Research Communications, 1981
- Studies on the Lysine-Binding Sites of Human Plasminogen. The Effect of Ligand Structure on the Binding of Lysine Analogs to PlasminogenEuropean Journal of Biochemistry, 1980