COMPUTATIONAL SEQUENCE-ANALYSIS OF MATRIX METALLOPROTEINASES

Matrix metalloproteinases (MMP) play a cardinal role in the breakdown of extracellular matrix involved in a variety of biological and pathol ogical processes. Research on MMPs has classified and characterized th ese enzymes according to their matrix substrate specificity, gene and protein domain structure, and regulation of activity and expression. H owever, the discovery of new MMPs has introduced a need for a more com prehensive and systematic method of classification and quantitative co mparison of known and newly discovered members. This study compiles a sequence alignment, constructs a dendrogram, and calculates physical d ata and homology percentage assignments in order to obtain further ins ight into MMP structure-function relationships. Thorough analysis of M MP primary sequence domains, physical data patterns, and statistical a nalysis of sequence homology yields higher resolution in the similarit ies and differences that group MMP members.