Sang Q A, Douglas D A
Department of Chemistry, Florida State University, Tallahassee 32306-3006, USA.
J Protein Chem. 1996 Feb;15(2):137-60. doi: 10.1007/BF01887395.
Matrix metalloproteinases (MMP) play a cardinal role in the breakdown of extracellular matrix involved in a variety of biological and pathological processes. Research on MMPs has classified and characterized these enzymes according to their matrix substrate specificity, gene and protein domain structure, and regulation of activity and expression. However, the discovery of new MMPs has introduced a need for a more comprehensive and systematic method of classification and quantitative comparison of known and newly discovered members. This study compiles a sequence alignment, constructs a dendrogram, and calculates physical data and homology percentage assignments in order to obtain further insight into MMP structure-function relationships. Thorough analysis of MMP primary sequence domains, physical data patterns, and statistical analysis of sequence homology yields higher resolution in the similarities and differences that group MMP members.
基质金属蛋白酶(MMP)在参与多种生物和病理过程的细胞外基质降解中起主要作用。对MMP的研究已根据其基质底物特异性、基因和蛋白质结构域结构以及活性和表达调控对这些酶进行了分类和表征。然而,新MMP的发现使得需要一种更全面、系统的方法来对已知和新发现的成员进行分类和定量比较。本研究编制了序列比对,构建了树状图,并计算了物理数据和同源百分比赋值,以便进一步深入了解MMP的结构-功能关系。对MMP一级序列结构域、物理数据模式进行全面分析,以及对序列同源性进行统计分析,能更清晰地揭示MMP成员之间的异同。