1ept
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(New page: 200px<br /><applet load="1ept" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ept, resolution 1.8Å" /> '''REFINED 1.8 ANGSTROMS...)
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Revision as of 12:05, 20 November 2007
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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 with CA as ligand. Active as Trypsin, with EC number 3.4.21.4 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 Tue Nov 20 14:12:53 2007
Categories: Protein complex | Sus scrofa | Trypsin | Huang, Q. | Li, Y. | Liu, S. | Tang, Y. | Wang, Z. | CA | Hydrolase (serine protease)
