Da. Douglas et al., COMPUTATIONAL SEQUENCE-ANALYSIS OF THE TISSUE INHIBITOR OF METALLOPROTEINASE FAMILY, Journal of protein chemistry, 16(4), 1997, pp. 237-255
The tissue inhibitor of metalloproteinase (TIMP) family regulates extr
acellular matrix turnover and tissue remodeling by forming tight-bindi
ng inhibitory complexes with matrix metalloproteinases (MMPs). MMPs an
d TIMPs have been implicated in many normal and pathological processes
, such as morphogenesis, development, angiogenesis, and cancer metasta
sis. This minireview provides information that would aid in classifica
tion of the TIMP family and in understanding the similarities and diff
erences among TIMP members according to the physical data, primary str
ucture, and homology values. Calculations of molecular weight, isoelec
tric point values, and molar extinction coefficients are reported. Thi
s study also compares sequence similarities and differences among the
TIMP members through calculations of homology within their individual
loop regions and the mature region of the molecule. Lastly, this repor
t examines structure-function relationships of TIMPs. Thorough knowled
ge of TIMP primary and tertiary structure would facilitate the uncover
ing of the molecular mechanisms underlying metalloproteinase, inhibito
ry activities and biological functions of TIMPs.