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Disorder-to-order conformational transitions in protein structure and its relationship to disease

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Abstract

Function in proteins largely depends on the acquisition of specific structures through folding at physiological time scales. Under both equilibrium and non-equilibrium states, proteins develop partially structured molecules that being intermediates in the process, usually resemble the structure of the fully folded protein. These intermediates, known as molten globules, present the faculty of adopting a large variety of conformations mainly supported by changes in their side chains. Taking into account that the mechanism to obtain a fully packed structure is considered more difficult energetically than forming partially “disordered” folding intermediates, evolution might have conferred upon an important number of proteins the capability to first partially fold and—depending on the presence of specific partner ligands—switch on disorder-to-order transitions to adopt a highly ordered well-folded state and reach the lowest energy conformation possible. Disorder in this context can represent segments of proteins or complete proteins that might exist in the native state. Moreover, because this type of disorder-to-order transition in proteins has been found to be reversible, it has been frequently associated with important signaling events in the cell. Due to the central role of this phenomenon in cell biology, protein misfolding and aberrant disorder-to-order transitions have been at present associated with an important number of diseases.

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Acknowledgments

Research described in this article carried out during the last few years in the laboratory of JM-O has been supported by Consejo Nacional de Ciencia y Tecnología, México (CONACyT-México) grant 47333/A-1 and by Universidad Nacional Autónoma de México (DGAPA-UNAM) grant IN228607. We want to thank Blanca Delgado-Coello for her technical help and Jorge Bravo-Martínez for his work in visualization and structure analysis, Mrs. Margaret Brunner for editorial services and Ma. Elena Gutierrez for manuscript preparation.

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  1. Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, Apdo. Postal 70-243, 04510, Mexico, D.F., Mexico

    Paola Mendoza-Espinosa, Victor García-González & Jaime Mas-Oliva

  2. Instituto de Química, Universidad Nacional Autónoma de México, Mexico, D.F., Mexico

    Abel Moreno

  3. Instituto de Física, Universidad Nacional Autónoma de México, Mexico, D.F., Mexico

    Rolando Castillo

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  1. Paola Mendoza-Espinosa
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  2. Victor García-González
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  3. Abel Moreno
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  5. Jaime Mas-Oliva
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Correspondence to Jaime Mas-Oliva.

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Mendoza-Espinosa, P., García-González, V., Moreno, A. et al. Disorder-to-order conformational transitions in protein structure and its relationship to disease. Mol Cell Biochem 330, 105–120 (2009). https://doi.org/10.1007/s11010-009-0105-6

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