Trimeresurus stejnegeri Snake Venom Plasminogen Activator. SITE-DIRECTED MUTAGENESIS AND MOLECULAR MODELING (original) (raw)
1997, Journal of Biological Chemistry
Related papers
Crystal Structure of the Proenzyme Domain of Plasminogen † , ‡
Biochemistry, 1999
We have solved the X-ray crystal structure of the proenzyme form of the catalytic domain of plasminogen, with the nonessential mutations M585Q, V673M, and M788L, to 2.0 A resolution. The structure presents an inactive protease characterized by Asp740 (chymotrypsinogen 194) hydrogen bonded to His586 (chymotrypsinogen 40), preventing proper formation of the oxyanion hole and S1 specificity pocket. In addition, the catalytic triad residues are misplaced relative to the active conformation adopted by serine proteases in the chymotrypsin family. Finally, a unique form of zymogen inactivation is observed, characterized by a "foot-in-mouth" mechanism in which Trp761 (chymotrypsinogen 215) is folded into the S1 specificity pocket preventing substrate binding.
Loading Preview
Sorry, preview is currently unavailable. You can download the paper by clicking the button above.