Bioinformatic comparison of structures and homology-models of matrix metalloproteinases.

摘要: The entire family of human matrix metalloproteinases (MMPs) was investigated using phylogenetic trees and homology modeling. analysis indicates that individual domains each MMP have evolved in a correlated manner. Despite their high sequence similarity, the tree catalytic already allows functional (e.g., linked to regulation substrate recognition) homologies between different MMPs be identified. same pattern is confirmed by mature proteins. Structural models were built for family, twelve hemopexin surface properties around active site cleft modeled experimental structures are quite conserved, whereas more differentiated, possibly indicating role determining specificity. showed area interface essentially with both hydrophobic hydrophilic amino acids at interface. absence specific conserved interdomain contacts suggests tolerant acid replacements, there may certain degree plasticity respect reciprocal orientation two domains.