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1ept
From Proteopedia
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'''REFINED 1.8 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF PORCINE EPSILON-TRYPSIN''' | '''REFINED 1.8 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF PORCINE EPSILON-TRYPSIN''' | ||
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[[Category: Tang, Y.]] | [[Category: Tang, Y.]] | ||
[[Category: Wang, Z.]] | [[Category: Wang, Z.]] | ||
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Revision as of 12:23, 2 May 2008
REFINED 1.8 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF PORCINE EPSILON-TRYPSIN
Overview
Porcine epsilon-trypsin is a three-chain inactivated trypsin from the limited autolysis of porcine beta-trypsin. It is cleaved at positions Lys60-Ser61 and Lys145-Ser146. The crystal structure has been determined by using the molecular replacement method, and refined at 1.8 A resolution. The R-value of final model is 0.184. Comparison with the electron density map of porcine beta-trypsin (PTRY) in complex (BBIT), and with that of native bovine beta-trypsin (HTNA), revealed no obvious changes except at the autolysis positions, and no changes at the active center were observed. The autolysis at positions Lys60-Ser61 and Lys145-Ser146 does not affect the conformation of His-57 in the active center and therefore cannot explain for a loss in porcine epsilon-trypsin activity.
About this Structure
1EPT is a Protein complex structure of sequences from Sus scrofa. Full crystallographic information is available from OCA.
Reference
Refined 1.8 A resolution crystal structure of the porcine epsilon-trypsin., Huang Q, Wang Z, Li Y, Liu S, Tang Y, Biochim Biophys Acta. 1994 Nov 16;1209(1):77-82. PMID:7947985 Page seeded by OCA on Fri May 2 15:23:07 2008
Categories: Protein complex | Sus scrofa | Trypsin | Huang, Q. | Li, Y. | Liu, S. | Tang, Y. | Wang, Z.
