Matrix metalloproteinases: structures, evolution, and diversification

摘要: A comprehensive sequence alignment of 64 members the family matrix metalloproteinases (MMPs) for entire sequences, and subsequently catalytic hemopexin-like domains, have been performed. The MMPs were selected from plants, invertebrates, vertebrates. analyses disclosed that as many 23 distinct subfamilies these proteins are known to exist. Information alignments was correlated with structures, both crystallographic well computational, domains representative MMP family. survey metal binding sites two loops containing variable sequences amino acids, which important substrate interactions, discussed. collective data support proposal assembly into multidomain enzymes likely be an early evolutionary event. This followed by diversification, perhaps in parallel among MMPs, a subsequent time scale. Analysis indicates retrograde structure simplification may accounted evolution simple domain constituents, such matrilysin, larger more elaborate enzymes.