Related Experiment Video

Updated: Jun 22, 2025

Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features
07:09

Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features

Published on: March 16, 2022

2.5K

Structural analysis of the FERM domain of human protein tyrosine phosphatase non-receptor type 21

Hye Seon Lee1, Bonsu Ku1, Ho Cheol Shin2

  • 1Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141, Republic of Korea.

Acta Crystallographica. Section F, Structural Biology Communications
|June 28, 2024
PubMed

Insights

Protein tyrosine phosphatase non-receptor type 21 (PTPN21) is a cancer therapeutic target. Researchers determined the PTPN21 FERM domain structure, revealing conserved folding and potential protein-binding sites for therapeutic development.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Oncology

Background:

  • Protein tyrosine phosphatase non-receptor type 21 (PTPN21) is a cytosolic enzyme implicated in cell growth and invasion.
  • PTPN21's oncogenic properties position it as a promising therapeutic target for various cancers.

Purpose of the Study:

  • To elucidate the three-dimensional structure of the PTPN21 FERM domain.
  • To identify potential protein-binding sites within the FERM domain for therapeutic intervention.

Main Methods:

  • X-ray crystallography was employed to determine the PTPN21 FERM domain structure at 2.1 Å resolution.
  • Structural analysis and superimposition were performed to compare PTPN21 FERM with other known FERM domains.

Main Results:

  • The crystal structure revealed canonical FERM folding, comprising three subdomains stabilized by conserved hydrophobic interactions.
  • High structural homology was observed between the PTPN21 FERM domain and other FERM domains.
  • Two putative protein-binding sites were identified, suggesting interaction with partners like kinesin family member 1C.

Conclusions:

  • The PTPN21 FERM domain functions as a crucial module for mediating protein-protein interactions.
  • Structural insights into the PTPN21 FERM domain can guide the development of targeted cancer therapies.
Keywords:
FERM domainsPTPN21cancer therapycrystal structureprotein tyrosine phosphatase non-receptor type 21protein-binding selectivity

More Related Videos

Quantitative FRET Förster Resonance Energy Transfer Analysis for SENP1 Protease Kinetics Determination16:02

Quantitative FRET Förster Resonance Energy Transfer Analysis for SENP1 Protease Kinetics Determination

Published on: February 21, 2013

19.0K
In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes10:05

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes

Published on: August 13, 2012

11.3K

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...
13.1K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
10.8K
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...
12.7K
Lipids as Anchors01:32

Lipids as Anchors

In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains...
5.6K