Sandbox Reserved 1125: Difference between revisions
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=== Homopexin domain === | === Homopexin domain === | ||
The hemopexin domain has two conserved cysteines that are disulfide bonded. Mutation of those cysteines to alanines | The hemopexin domain has two conserved cysteines that are disulfide bonded. Mutation of those cysteines to alanines <ref>PMID:8464863</ref> or reduction and alkylation destroys collagenolytic activity (K. Suzuki and H.Nagase, unpublished results).<ref name="Pdf"/> | ||
== Mechanism == | == Mechanism == | ||
To express collagenolytic activity, they have to retain both the catalytic and hemopexin domains. | To express collagenolytic activity, they have to retain both the catalytic and hemopexin domains. | ||
It is not clear how the hemopexin domain help to cleave triple-helical collagens because the isolated hemopexin domains of MMP-8 does not bind to collagen.<ref>PMID:8489511</ref> | It is not clear how the hemopexin domain help to cleave triple-helical collagens because the isolated hemopexin domains of MMP-8 does not bind to collagen.<ref>PMID:8489511</ref> | ||
The binding of collagenases to collagen must partially unwind triple helix to allow cleavage of the individual � chains. Since heat-denatured collagens (gelatins) are poorer substrates at 37°C <ref>PMID:6270090</ref>, interaction of collagenase to interstitial collagen must induce conformational change in alpha chain of collagen that fits the substrate bind. | |||
