Sandbox Reserved 1125: Difference between revisions

From Proteopedia
Jump to navigationJump to search
No edit summary
No edit summary
Line 64: Line 64:
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.
The binding of collagenases to collagen must partially unwind triple helix to allow cleavage of the individual alpha 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 binding site of the catalytic domain, but the molecular basis of this mechanism is not known.