Computational sequence analysis of the tissue inhibitor of metalloproteinase family.
The tissue inhibitor of metalloproteinase (TIMP) family regulates extracellular matrix turnover and tissue remodeling by forming tight-binding inhibitory complexes with matrix metalloproteinases (MMPs). MMPs and TIMPs have been implicated in many normal and pathological processes, such as morphogenesis, development, angiogenesis, and cancer metastasis. This minireview provides information that would aid in classification of the TIMP family and in understanding the similarities and differences among TIMP members according to the physical data, primary structure, and homology values. Calculations of molecular weight, isoelectric point values, and molar extinction coefficients are reported. This 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 report examines structure-function relationships of TIMPs. Thorough knowledge of TIMP primary and tertiary structure would facilitate the uncovering of the molecular mechanisms underlying metalloproteinase, inhibitory activities and biological functions of TIMPs.
Douglas
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Department of Chemistry, Florida State University, Tallahassee 32306-3006, USA.
Shi
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Sang
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D000465:Algorithms; D000595:Amino Acid Sequence; D000818:Animals; D006023:Glycoproteins / Q000737:chemistry* / Q000235:genetics; D006801:Humans; D061965:Matrix Metalloproteinase Inhibitors; D008969:Molecular Sequence Data; D005810:Multigene Family; D017421:Sequence Analysis / Q000379:methods*; D017386:Sequence Homology, Amino Acid; D019714:Tissue Inhibitor of Metalloproteinases
D006023:Glycoproteins; D061965:Matrix Metalloproteinase Inhibitors; D019714:Tissue Inhibitor of Metalloproteinases