1ecz: Difference between revisions

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[[Image:1ecz.jpg|left|200px]]
{{Seed}}
[[Image:1ecz.png|left|200px]]


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{{STRUCTURE_1ecz|  PDB=1ecz  |  SCENE=  }}  
{{STRUCTURE_1ecz|  PDB=1ecz  |  SCENE=  }}  


'''PROTEASE INHIBITOR ECOTIN'''
===PROTEASE INHIBITOR ECOTIN===




==Overview==
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Ecotin, a homodimeric protein composed of 142 residue subunits, is a novel serine protease inhibitor present in Escherichia coli. Its thermostability and acid stability, as well as broad specificity toward proteases, make it an interesting protein for structural characterization. Its structure in the uncomplexed state, determined for two different crystalline environments, allows a structural comparison of the free inhibitor with that in complex with trypsin. Although there is no gross structural rearrangement of ecotin when binding trypsin, the loops involved in binding trypsin show relatively large shifts in atomic positions. The inherent flexibility of the loops and the highly nonglobular shape are the two features essential for its inhibitory function. An insight into the understanding of the structural basis of thermostability and acid stability of ecotin is also provided by the present structure.
The line below this paragraph, {{ABSTRACT_PUBMED_8931142}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_8931142}}


==About this Structure==
==About this Structure==
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[[Category: Periplasmic]]
[[Category: Periplasmic]]
[[Category: Serine protease inhibitor]]
[[Category: Serine protease inhibitor]]
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Revision as of 21:30, 30 June 2008

File:1ecz.png

Template:STRUCTURE 1ecz

PROTEASE INHIBITOR ECOTIN

Template:ABSTRACT PUBMED 8931142

About this Structure

1ECZ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure analyses of uncomplexed ecotin in two crystal forms: implications for its function and stability., Shin DH, Song HK, Seong IS, Lee CS, Chung CH, Suh SW, Protein Sci. 1996 Nov;5(11):2236-47. PMID:8931142

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