1ekb

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{{STRUCTURE_1ekb| PDB=1ekb | SCENE= }}
{{STRUCTURE_1ekb| PDB=1ekb | SCENE= }}
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'''THE SERINE PROTEASE DOMAIN OF ENTEROPEPTIDASE BOUND TO INHIBITOR VAL-ASP-ASP-ASP-ASP-LYS-CHLOROMETHANE'''
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===THE SERINE PROTEASE DOMAIN OF ENTEROPEPTIDASE BOUND TO INHIBITOR VAL-ASP-ASP-ASP-ASP-LYS-CHLOROMETHANE===
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==Overview==
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Enteropeptidase is a membrane-bound serine protease that initiates the activation of pancreatic hydrolases by cleaving and activating trypsinogen. The enzyme is remarkably specific and cleaves after lysine residues of peptidyl substrates that resemble trypsinogen activation peptides such as Val-(Asp)4-Lys. To characterize the determinants of substrate specificity, we solved the crystal structure of the bovine enteropeptidase catalytic domain to 2.3 A resolution in complex with the inhibitor Val-(Asp)4-Lys-chloromethane. The catalytic mechanism and contacts with lysine at substrate position P1 are conserved with other trypsin-like serine proteases. However, the aspartyl residues at positions P2-P4 of the inhibitor interact with the enzyme surface mainly through salt bridges with the Nzeta atom of Lys99. Mutation of Lys99 to Ala, or acetylation with acetic anhydride, specifically prevented the cleavage of trypsinogen or Gly-(Asp)4-Lys-beta-naphthylamide and reduced the rate of inhibition by Val-(Asp)4-Lys-chloromethane 22 to 90-fold. For these reactions, Lys99 was calculated to account for 1.8 to 2.5 kcal mol(-1) of the free energy of transition state binding. Thus, a unique basic exosite on the enteropeptidase surface has evolved to facilitate the cleavage of its physiological substrate, trypsinogen.
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(as it appears on PubMed at http://www.pubmed.gov), where 10493881 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10493881}}
==About this Structure==
==About this Structure==
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[[Category: Enteropeptidase]]
[[Category: Enteropeptidase]]
[[Category: Trypsinogen activation]]
[[Category: Trypsinogen activation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:53:08 2008''

Revision as of 21:53, 30 June 2008

Image:1ekb.png

Template:STRUCTURE 1ekb

THE SERINE PROTEASE DOMAIN OF ENTEROPEPTIDASE BOUND TO INHIBITOR VAL-ASP-ASP-ASP-ASP-LYS-CHLOROMETHANE

Template:ABSTRACT PUBMED 10493881

About this Structure

1EKB is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

Reference

Crystal structure of enteropeptidase light chain complexed with an analog of the trypsinogen activation peptide., Lu D, Futterer K, Korolev S, Zheng X, Tan K, Waksman G, Sadler JE, J Mol Biol. 1999 Sep 17;292(2):361-73. PMID:10493881

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