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Related Concept Videos

Phosphorylation01:02

Phosphorylation

53.2K
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...
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Calmodulin-dependent Signaling01:16

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 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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Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

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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...
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Assembly of Signaling Complexes01:30

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.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
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Related Experiment Video

Updated: Dec 7, 2025

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein
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Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

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Conformational states dynamically populated by a kinase determine its function.

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
PubMed
Summary

Protein kinases switch between active and inactive states. Understanding these conformational changes in Abl kinase reveals how mutations activate cancer and how drugs like imatinib work, aiding new inhibitor design.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Protein kinases possess dynamic conformational states influencing their activity.
  • Abl kinase, a key regulator, undergoes transitions between active and inactive forms.

Purpose of the Study:

  • To elucidate the atomic-level conformational dynamics of Abl kinase.
  • To understand the regulatory mechanisms governing kinase activity and drug interactions.

Main Methods:

  • Nuclear magnetic resonance (NMR) spectroscopy was employed.
  • Detailed structural analysis of distinct conformational states.

Main Results:

  • Abl kinase interconverts between active and two distinct inactive states.
  • Differences in structural elements like the activation loop and DFG motif drive regulation.
  • Imatinib binding site and resistance mechanisms were characterized.

Conclusions:

  • Kinase conformational flexibility underlies intrinsic regulation and oncogenic activation.
  • Structural insights into inactive states can guide the development of selective inhibitors.