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Phosphorylation

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...

Calmodulin-dependent Signaling

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Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...

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Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
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When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...

Assembly of Signaling Complexes

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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
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Los estados conformacionales poblados dinámicamente por una quinasa determinan su función

Tao Xie¹, Tamjeed Saleh¹, Paolo Rossi¹

¹Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN, USA.

Science (New York, N.Y.)

|October 2, 2020

Resumen

Las proteínas quinasas cambian entre estados activos e inactivos. Comprender estos cambios conformacionales en la Abl quinasa revela cómo las mutaciones activan el cáncer y cómo funcionan medicamentos como el imatinib, ayudando al diseño de nuevos inhibidores.

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Área de la Ciencia:

La bioquímica
Biología estructural
Biología molecular

Sus antecedentes:

Las proteínas quinasas poseen estados conformacionales dinámicos que influyen en su actividad.
La Abl quinasa, un regulador clave, sufre transiciones entre formas activas e inactivas.

Objetivo del estudio:

Para aclarar la dinámica conformacional a nivel atómico de la Abl quinasa.
Comprender los mecanismos reguladores que rigen la actividad de la quinasa y las interacciones farmacológicas.

Principales métodos:

Se empleó la espectroscopia de resonancia magnética nuclear (RMN).
Análisis estructural detallado de estados conformacionales distintos.

Principales resultados:

La Abl quinasa interconvierte entre dos estados activos e inactivos distintos.
Diferencias en elementos estructurales como el bucle de activación y la regulación de la unidad de motivo DFG.
Se caracterizaron el sitio de unión de imatinib y los mecanismos de resistencia.

Conclusiones:

La flexibilidad conformacional de la quinasa subyace a la regulación intrínseca y a la activación oncogénica.
Las ideas estructurales sobre los estados inactivos pueden guiar el desarrollo de inhibidores selectivos.