1qrz
From Proteopedia
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Revision as of 14:58, 5 November 2007
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CATALYTIC DOMAIN OF PLASMINOGEN
Overview
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.
About this Structure
1QRZ is a Single protein structure of sequence from Homo sapiens. Structure known Active Sites: ACA, ACB, ACC and ACD. Full crystallographic information is available from OCA.
Reference
Crystal structure of the proenzyme domain of plasminogen., Peisach E, Wang J, de los Santos T, Reich E, Ringe D, Biochemistry. 1999 Aug 24;38(34):11180-8. PMID:10460175
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