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Related Concept Videos

Protein Kinases and Phosphatases02:54

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
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein Kinases and Phosphatases02:54

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
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Phosphorylation01:02

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...
Phosphorylation01:02

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...
Receptor Tyrosine Kinases01:26

Receptor Tyrosine Kinases

Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:

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Related Experiment Video

Updated: Jul 7, 2026

Assessing Cellular Target Engagement by SHP2 (PTPN11) Phosphatase Inhibitors
08:45

Assessing Cellular Target Engagement by SHP2 (PTPN11) Phosphatase Inhibitors

Published on: July 17, 2020

Protein tyrosine phosphatases: structure-function relationships.

Lydia Tabernero1, A Radu Aricescu, E Yvonne Jones

  • 1Faculty of Life Sciences, University of Manchester, UK. Lydia.Tabernero@manchester.ac.uk

The FEBS Journal
|February 27, 2008
PubMed
Summary
This summary is machine-generated.

Structural analysis of protein tyrosine phosphatases (PTPs) reveals enzyme architecture and regulation. This structural data aids in understanding PTPs

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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

Area of Science:

  • Biochemistry and Structural Biology
  • Enzymology
  • Molecular Medicine

Background:

  • Protein tyrosine phosphatases (PTPs) are crucial enzymes involved in cellular signaling.
  • Over 200 structures of PTPs and their complexes have been determined, offering insights into their function.
  • PTPs are implicated in diseases like diabetes and cancer, making them therapeutic targets.

Purpose of the Study:

  • To review prominent structural traits of PTPs and their ligand complexes.
  • To discuss the implications of PTP structural data for functional studies and drug design.
  • To highlight advancements in PTP structural biology, including receptor-like PTPs.

Main Methods:

  • Compilation and analysis of existing PTP structural data from crystallographic and NMR studies.
  • Review of mammalian expression technologies enabling structural determination of complex PTPs.
  • Integration of structural findings with biological function and therapeutic relevance.

Main Results:

  • The catalytic domain size and compact fold of PTPs facilitate structural analysis.
  • Structural data reveals insights into PTP architecture, regulation, and substrate specificity.
  • Recent advancements include the first crystal structure of a receptor-like PTP extracellular region.

Conclusions:

  • PTP structural biology has significantly advanced our understanding of these enzymes.
  • Structural information is vital for designing functional experiments and developing PTP-targeted drugs.
  • PTPs represent strategic targets for therapeutic intervention in human diseases.