Allosteric proteins and

Monod J, Changeux J-P, Jacob F. Allosteric proteins and cellular control systems. J Mol Biol 1963 6 308-329. 

Haemoglobin is one of the most well studied and best understood proteins thanks largely to the early work of Max Perutz, John Kendrew and colleagues. Haemoglobin is now often used as a model allosteric protein and to illustrate the impact of protein structural alterations in disease. 

Monod, J., Changeux, J.P, Jacob, F. (1963). Allosteric proteins and cellular control processes. J. Mol. Biol. 6, 306-329. 

The role of certain enzymes in cell control and human disease has also received attention, especially in regard to the specificity of enzymes and to protein phosphatases.200 There has also been intense interest in biocatalysis as an application of enzyme chemistry in organic synthesis,201 in the uses of proteolytic enzymes as shown by the work of Perutz,202 and in nucleotide enzymology.203 New methods of investigating the complexities of enzyme action have been described,204,205 as have new methods of determining enzyme structures using studies of bacterial nutrition.206 Other studies have investigated the relations between allosteric proteins and enzymes,207 and the mechanisms by which they function. 

J. Monod, J.-P. Changeux, and E Jacob Allosteric proteins and cellular control systems. Journal of Molecular Biology 6, 306 (1963). 

Despite the difficulty in obtaining structural information for each allosteric state in any given protein or receptor, drug discovery with allosteric systems is well under way and bearing fruit. The purpose of this chapter is to review the underlying principles of allosteric proteins and how these may be used to design "allosteric" drugs. 

The key to allosteric behavior, including cooperativity and modifications of cooperativity, is the existence of multiple forms for the quaternary structures of allosteric proteins. The word allosteric is, derived from alio, other, and stetic, shape, referring to the fact that the possible conformations affect the behavior of the protein. The binding of substrates, inhibitors, and activators changes the quaternary structure of allosteric proteins, and the changes in structure are reflected in the behavior of those proteins. A substance that modifies the quaternary structure, and thus the behavior, of an allosteric protein by binding to it is called an allosteric effector. The term effector can apply to substrates, inhibitors, or activators. Several models for the behavior of allosteric enzymes have been proposed, and it is worthwhile to compare them. 

Kenakin, T. P. (2010). G protein coupled receptors as allosteric proteins and the role of allosteric modulators. Joumfl/ of Receptor and Signal Transduction Research, 30, 313-321. 

The case of allosteric proteins and of their conformational properties is interesting with many respects. For proteins obeying the model of Monod et al (1965), a pre-equilibrium between two active conformations is involved with an allosteric constant Lq such that Lq = This value... 

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