Function of the central domain of streptokinase in substrate plasminogen docking and processing revealed by site-directed mutagenesis

• Published in: Protein science Vol. 8; no. 12; pp. 2791 - 2805
• Main Authors: CHAUDHARY, ANITA, VASUDHA, S., RAJAGOPAL, K., KOMATH, SNEHA SUDHA, GARG, NANDITA, YADAV, M., MANDE, SHEKHAR C., SAHNI, GIRISH
• Format: Journal Article
• Language: English
• Published: Bristol Cambridge University Press 01.12.1999; Cold Spring Harbor Laboratory Press
• Subjects: Amino Acid Sequence; Base Sequence; Circular Dichroism; Escherichia coli - metabolism; Humans; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; plasminogen; Plasminogen - chemistry; Plasminogen - metabolism; plasminogen activation mechanism; Plasminogen Activators - chemistry; Plasminogen Activators - genetics; Plasminogen Activators - metabolism; Protein Structure, Tertiary; site‐specific mutagenesis; streptokinase; Streptokinase - chemistry; Streptokinase - genetics; Streptokinase - metabolism; substrate plasminogen; plasminogen; streptokinase; plasminogen activation mechanism; site-specific mutagenesis; substrate plasminogen

The possible role of the central β-domain (residues 151–287) of streptokinase (SK) was probed by site-specifically altering two charged residues at a time to alanines in a region (residues 230–290) previously identified by Peptide Walking to play a key role in plasminogen (PG) activation. These muta...