The solution structure of the human plasminogen kringle 1 domain complexed to the antifibrinolytic drug 6-aminohexanoic acid (epsilon Ahx) was obtained on the basis of 1H-NMR spectroscopic data and dynamical simulated annealing calculations.
With the presence of disulfide bonds, plasminogen's structure is divided into a contiguous series of five homologous regions called kringles.
Plasminogen is converted to plasmin by cleavage of Lys-77 releasing the N-terminal peptide.
Plasminogen Description: Plasminogen, a single chain glycoprotein zymogen, is the precursor the fibrinolytic enzyme plasmin.
The native form of plasminogen is composed of 791 amino acids with glutamic acid located at the N-terminal portion (Glu-plasminogen).
Plasminogen is converted to plasmin via a cascade of various reactions that result in the hydrolysis of Arg560-Val561 peptide bond of plasminogen resulting in two chains that remain covalently associated by a disulfide bond.
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