title: Computational sequence analysis of matrix metalloproteinases.
abstract: 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.
authors.affiliation: Department of Chemistry, Florida State University, Tallahassee 32306-3006, USA. SANG@Chem.FSU.EDU
authors.forename: Q A
authors.initials: QA
authors.lastname: Sang
authors.forename: D A
authors.initials: DA
authors.lastname: Douglas
mesh_terms: D000465:Algorithms; D000595:Amino Acid Sequence; D007526:Isoelectric Point; D008666:Metalloendopeptidases / Q000737:chemistry* / Q000145:classification; D008969:Molecular Sequence Data; D008970:Molecular Weight; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
chemical_list: D008666:Metalloendopeptidases