A computer-assisted three dimensional model of the copper-containing enzyme lysyl oxidase (LOX), whose primary function is to maintain the structural integrity of the extracellular matrices, has recently been created. This computer generated model, validated through a series of in vitro experiments, allows for further study of enzyme inhibition and substrate action at the molecular level. Limited data was presented before regarding the interactions between LOX and small substrates and inhibitors, but not for larger natural substrates such as collagen and elastin. Newly published crystallographic structures of procollagen and elastin allowed the effects of interactions between LOX and these two native biopolymers to be studied. Questions regarding what interactions between LOX and its natural substrates occur, which of them are crucial for the enzyme's action, and how these interactions may be used for the future design of specific inhibitors and substrates of LOX will be discussed.

Computational investigation of the interactions of lysyl oxidase with its natural substrates

245th National Meeting (2013)

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