Substitution of arginine 719 for glutamic acid in human plasminogen substantially reduces its affinity for streptokinase

Glu) in the serine protease domain of full-length Glu-plasminogen substantially reduces its affinity for streptokinase. The plasminogen variant displays no other significant differences from the wild-type molecule with respect to activation by two-chain urokinase-type plasminogen activator, recognition by monoclonal antibodies, or ability to undergo conformational change. It is concluded that Arg719 in human plasminogen is an important determinant of the streptokinase binding site, although further sites are likely to contribute both to the affinity of plasminogen for streptokinase and to mechanisms by which the active site is formed within the complex. -->

ISSN:	0006-2960
Přístupová URL adresa:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::215af9dcbdeb28e3bca6c357cc5fa908 https://pubmed.ncbi.nlm.nih.gov/7918423
Přírůstkové číslo:	edsair.doi.dedup.....215af9dcbdeb28e3bca6c357cc5fa908
Autor:	Keith Martyn Dawson, Julian M. Marshall, Richard James Gilbert, Robert H. Raper, Chris P. Ponting
Rok vydání:	1994
Předmět:	Models Molecular Conformational change Arginine Protein Conformation Streptokinase Molecular Sequence Data Oligonucleotides Glutamic Acid Enzyme-Linked Immunosorbent Assay CHO Cells Biochemistry Plasminogen Activators Cricetinae medicine Animals Humans Binding site Chromatography High Pressure Liquid Serine protease Binding Sites biology Base Sequence Serine Endopeptidases Active site Antibodies Monoclonal Plasminogen Glutamic acid Molecular biology Recombinant Proteins biology.protein Mutagenesis Site-Directed Plasminogen activator medicine.drug
Zdroj:	Biochemistry. 33(40)
ISSN:	0006-2960
Popis:	In isolation human plasminogen possesses no enzymatic activity, yet upon formation of an equimolar complex with the bacterial protein streptokinase, it acquires a plasminogen activator function. The region(s) of plasminogen and of streptokinase which mediate complex formation has (have) not been previously published. Here it is reported that a single-residue substitution (Arg719-->Glu) in the serine protease domain of full-length Glu-plasminogen substantially reduces its affinity for streptokinase. The plasminogen variant displays no other significant differences from the wild-type molecule with respect to activation by two-chain urokinase-type plasminogen activator, recognition by monoclonal antibodies, or ability to undergo conformational change. It is concluded that Arg719 in human plasminogen is an important determinant of the streptokinase binding site, although further sites are likely to contribute both to the affinity of plasminogen for streptokinase and to mechanisms by which the active site is formed within the complex.
Databáze:	OpenAIRE
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