1ezx

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[[Image:1ezx.gif|left|200px]]
[[Image:1ezx.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1ezx |SIZE=350|CAPTION= <scene name='initialview01'>1ezx</scene>, resolution 2.60&Aring;
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The line below this paragraph, containing "STRUCTURE_1ezx", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span>
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_1ezx| PDB=1ezx | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ezx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ezx OCA], [http://www.ebi.ac.uk/pdbsum/1ezx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ezx RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF A SERPIN:PROTEASE COMPLEX'''
'''CRYSTAL STRUCTURE OF A SERPIN:PROTEASE COMPLEX'''
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[[Category: Carrell, R W.]]
[[Category: Carrell, R W.]]
[[Category: Huntington, J A.]]
[[Category: Huntington, J A.]]
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[[Category: alpha-1-antitrypsin]]
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[[Category: Alpha-1-antitrypsin]]
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[[Category: protease-inhibitor complex]]
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[[Category: Protease-inhibitor complex]]
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[[Category: serpin]]
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[[Category: Serpin]]
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[[Category: trypsin]]
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[[Category: Trypsin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:43:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:13:03 2008''
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Revision as of 12:43, 2 May 2008

Template:STRUCTURE 1ezx

CRYSTAL STRUCTURE OF A SERPIN:PROTEASE COMPLEX


Overview

The serpins have evolved to be the predominant family of serine-protease inhibitors in man. Their unique mechanism of inhibition involves a profound change in conformation, although the nature and significance of this change has been controversial. Here we report the crystallographic structure of a typical serpin-protease complex and show the mechanism of inhibition. The conformational change is initiated by reaction of the active serine of the protease with the reactive centre of the serpin. This cleaves the reactive centre, which then moves 71 A to the opposite pole of the serpin, taking the tethered protease with it. The tight linkage of the two molecules and resulting overlap of their structures does not affect the hyperstable serpin, but causes a surprising 37% loss of structure in the protease. This is induced by the plucking of the serine from its active site, together with breakage of interactions formed during zymogen activation. The disruption of the catalytic site prevents the release of the protease from the complex, and the structural disorder allows its proteolytic destruction. It is this ability of the conformational mechanism to crush as well as inhibit proteases that provides the serpins with their selective advantage.

About this Structure

1EZX is a Protein complex structure of sequences from Bos taurus and Homo sapiens. The following page contains interesting information on the relation of 1EZX with [Serpins]. Full crystallographic information is available from OCA.

Reference

Structure of a serpin-protease complex shows inhibition by deformation., Huntington JA, Read RJ, Carrell RW, Nature. 2000 Oct 19;407(6806):923-6. PMID:11057674 Page seeded by OCA on Fri May 2 15:43:27 2008

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