1ezx

CRYSTAL STRUCTURE OF A SERPIN:PROTEASE COMPLEX

spinqualitylabelsall models 1ezx, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ezx is a 3 chain structure with sequence from Bos taurus and Homo sapiens. The May 2004 RCSB PDB Molecule of the Month feature on Serpins by David S. Goodsell is 10.2210/rcsb_pdb/mom_2004_5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TRY1_BOVIN Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Alpha-1-antitrypsin 3D structures

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