1ept

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{{STRUCTURE_1ept| PDB=1ept | SCENE= }}
{{STRUCTURE_1ept| PDB=1ept | SCENE= }}
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'''REFINED 1.8 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF PORCINE EPSILON-TRYPSIN'''
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===REFINED 1.8 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF PORCINE EPSILON-TRYPSIN===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_7947985}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 7947985 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7947985}}
==About this Structure==
==About this Structure==
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[[Category: Tang, Y.]]
[[Category: Tang, Y.]]
[[Category: Wang, Z.]]
[[Category: Wang, Z.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:23:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 01:34:00 2008''

Revision as of 22:34, 30 June 2008

Image:1ept.png

Template:STRUCTURE 1ept

REFINED 1.8 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF PORCINE EPSILON-TRYPSIN

Template:ABSTRACT PUBMED 7947985

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

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