1c8t

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Revision as of 17:12, 12 November 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1c8t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c8t, resolution 2.60Å" /> '''HUMAN STROMELYSIN-1...)
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File:1c8t.gif


1c8t, resolution 2.60Å

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HUMAN STROMELYSIN-1 (E202Q) CATALYTIC DOMAIN COMPLEXED WITH RO-26-2812

OverviewOverview

Human stromelysin-1 is a member of the matrix metalloproteinase (MMP), family of enzymes. The active site glutamic acid of the MMPs is conserved, throughout the family and plays a pivotal role in the catalytic mechanism., The structural and functional consequences of a glutamate to glutamine, substitution in the active site of stromelysin-1 were investigated in this, study. In contrast to the wild-type enzyme, the glutamine-substituted, mutant was not active in a zymogram assay where gelatin was the substrate, was not activated by organomercurials and showed no activity against a, peptide substrate. The glutamine-substituted mutant did, however, bind to, TIMP-1, the tissue inhibitor of metalloproteinases, after cleavage of the, propeptide with trypsin. A second construct containing the glutamine, substitution but lacking the propeptide was also inactive in the, proteolysis assays and capable of TIMP-1 binding. X-ray structures of the, wild-type and mutant proteins complexed with the propeptide-based, inhibitor Ro-26-2812 were solved and in both structures the inhibitor, binds in an orientation the reverse of that of the propeptide in the, pro-form of the enzyme. The inhibitor makes no specific interactions with, the active site glutamate and a comparison of the wild-type and mutant, structures revealed no major structural changes resulting from the, glutamate to glutamine substitution.

DiseaseDisease

Known diseases associated with this structure: Coronary heart disease, susceptibility to OMIM:[185250]

About this StructureAbout this Structure

1C8T is a Single protein structure of sequence from Homo sapiens with ZN, CA and TR1 as ligands. Active as Stromelysin 1, with EC number 3.4.24.17 Full crystallographic information is available from OCA.

ReferenceReference

Expression, characterization and structure determination of an active site mutant (Glu202-Gln) of mini-stromelysin-1., Steele DL, El-Kabbani O, Dunten P, Windsor LJ, Kammlott RU, Crowther RL, Michoud C, Engler JA, Birktoft JJ, Protein Eng. 2000 Jun;13(6):397-405. PMID:10877850

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