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Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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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
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Structural Protein Function01:56

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Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
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cAMP-dependent Protein Kinase Pathways01:25

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Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
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Quantification of Bacterial Histidine Kinase Autophosphorylation Using a Nitrocellulose Binding Assay
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Structural Basis of Protein Kinase R Autophosphorylation.

Christopher B Mayo, Heidi Erlandsen, David J Mouser

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    The RNA-activated protein kinase, PKR, forms a novel front-to-front dimer structure, enabling trans-autophosphorylation crucial for innate immunity against viral infections.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Immunology

    Background:

    • RNA-activated protein kinase (PKR) mediates innate immunity.
    • Viral dsRNA triggers PKR dimerization and autophosphorylation.
    • The canonical PKR kinase domain dimer arrangement hinders intermolecular phosphorylation.

    Purpose of the Study:

    • To elucidate the structural basis of PKR autophosphorylation.
    • To resolve the dilemma of intermolecular phosphorylation in PKR dimers.
    • To propose a mechanism for PKR activation and function.

    Main Methods:

    • X-ray crystallography of PKR kinase domain structures.
    • Mutational analysis of PKR interfaces.
    • Molecular dynamics simulations.

    Main Results:

    • PKR kinase domains form a unique front-to-front dimer via activation segment exchange.
    • This novel interface is critical for PKR activation.
    • Simulations show dynamic activation segments facilitating phosphoryl transfer.

    Conclusions:

    • A new model for PKR activation involving back-to-back and front-to-front dimerization is proposed.
    • This mechanism explains how PKR achieves trans-autophosphorylation.
    • The findings may apply to related kinases involved in eIF2α phosphorylation.