The two faces of the proteins structure Application of knowledge about intrinsically disordered proteins in rational drug design
DOI:
https://doi.org/10.34767/SIMIS.2013.10.01Keywords:
molecular recognition features, protein protein interactions, protein folding, amino acid sequence properties of proteins.Abstract
Proteins are an essential component of living cells. Proper understanding of the properties of their structure is crucial to understanding their function in nature. The proteins and their fragments may exist in four states of structure organization: ordered, molten globule, pre molten globule and random coil. The particular function of proteins depend on any one of these states or a transition between
them. A significant proportion of proteins in nature is composed of a mixture of ordered and intrinsically disordered regions, that fulfil important roles in the processes like signal transduction, cell cycle regulation and many others. The standard approach for rational drug
design does not work for intrinsically disordered proteins (IDPs) and requires modified strategies. Furthermore, the majority of proteins with long intrinsically disordered regions (IDRs) use short molecular recognition elements (MoRFs), which undergo transition from disorder to
order state and adopt various structures in numerous protein protein interactions. These interactions are an attractive therapeutic target for the pharmaceutical industry in the process of rational drug design.
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