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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
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Related Experiment Video

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Assessing Cellular Target Engagement by SHP2 PTPN11 Phosphatase Inhibitors
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Cooperative dynamics across distinct structural elements regulate PTP1B activity.

Kristiane R Torgeson1, Michael W Clarkson1, Ganesan Senthil Kumar1

  • 1Department of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona, USA.

The Journal of Biological Chemistry
|August 2, 2020
PubMed
Summary

Protein-tyrosine phosphatase 1B (PTP1B) dynamics reveal coordinated loops crucial for its function. This study shows key elements work together, not independently, for PTP1B activity.

Keywords:
13C methyl ILV dynamicsNMR spectroscopyPTP1Bct-CPMGenzymeenzyme catalysisenzyme mechanismnuclear magnetic resonance (NMR)protein dynamicprotein-tyrosine phosphatase

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Protein-tyrosine phosphatase 1B (PTP1B) is a key enzyme for studying structure-function relationships.
  • Protein dynamics are known to be essential for PTP1B function, but their coordination remains unclear.

Purpose of the Study:

  • To investigate whether distinct structural elements of PTP1B function independently or are dynamically coordinated.
  • To understand the influence of protein motions on PTP1B catalytic activity across different timescales.

Main Methods:

  • Utilized a comprehensive 13C-methyl relaxation study of Ile, Leu, and Val (ILV) residues in PTP1B.
  • Employed 13C ILV constant-time Carr-Purcell-Meiboom-Gill relaxation measurements.

Main Results:

  • PTP1B exhibits dynamics on three distinct timescales, including slow motion of N-terminal helices.
  • Fast timescale dynamics of 13C-methyl side chains and 15N backbone are consistent, indicating their role in allosteric control.
  • Catalytically important loops (WPD, Q, E, substrate-binding) function in dynamic unity throughout the catalytic cycle.

Conclusions:

  • PTP1B activity is regulated by dynamically coordinated key elements, not a single functional component.
  • This study provides a comprehensive understanding of PTP1B function and its validated drug target status.