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H. TSCHESCHE and M. FARR
like pregnancy, embryonic development, angiogenesis, formation of bones and
organs, the remodelling of tissues, leukodiapedesis, wound healing and pathological processes like rheumatoid arthritis, osteoarthritis, parodontosis, multiple
sclerosis, tumor formation, metastasis, liver fibrosis, cystic fibrosis and aneurysm (for reviews see Birkedal-Hansen et a1. 1993). Because all MMPs have a conserved zinc binding motif (HExGHxxGxxH) and an adjacent l,4-tight "Met-turn"
they belong to the "metzincins" as a subgroup of metalloproteinases. They are
minimal domain M M P
Dt...._..:.. C .&...1 _---..::ZOll..D...J
MMPs \ ith hemopexin like domain
IMPs with transmcmbranc domain
M M Ps with libronectin like domain
o
signal pcptid
CTI propeptid
()
furin recognition site
CLiiJ catalytic domain
'\,
"hingc"-rcgion
Illalrily in ( MP-7)
collagcnae
(MMP-I.-'.-I.-18)
slromclysin
(MM P-3, -10)
I11c t alloelasta~e (M M P -1 2)
RA I-I
(MMP- 19)
cnamcly in
(M M pox)
X 1 P
(MMP-y)
stromclysin-3 (MMP-II)
membrane bound M M P s
( TI-. T2-. n-, MT4-MMP)
gclatinase A (MMP-2)
I...-........ ---'I...-........ --Ir gelatina e B (MMP-9)
hemopc.xin like domain
crD fibroncctin like domain
o lyp V collagen like domain
o Iran. membrane domain
Fig. 21.1. Domain structure of matrix metalloproteinases