Relating matrix metalloproteinase structure to function: why the "hemopexin" domain?
Matrix metalloproteinases are thought to be key players in the remodelling activity of cells associated with both physiological and pathological processes. They share a relatively conserved structure with a number of identifiable modules linked to their specific functions. The structure of the individual domains of a number of matrix metalloproteinases have now been elucidated. Here we review these data in the light of complementary studies on the behaviour of these enzymes in biological systems. In particular we focus on the C-terminal hemopexin-like domain which has intriguingly specific roles in individual matrix metalloproteinases.
Murphy
G
G
Strangeways Research Laboratory, Cambridge, United Kingdom.
Knäuper
V
V
D000595:Amino Acid Sequence; D000818:Animals; D017364:Collagenases / Q000737:chemistry / Q000378:metabolism; D005109:Extracellular Matrix / Q000201:enzymology*; D005353:Fibronectins / Q000737:chemistry; D006466:Hemopexin / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008666:Metalloendopeptidases / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation
D005353:Fibronectins; D006466:Hemopexin; D017364:Collagenases; D008666:Metalloendopeptidases