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Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
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The TRIM14 PRYSPRY domain mediates protein interaction via its basic interface.

Ying Yu1, Ling Liang1,2, Yan Jin1

  • 1Institute of Systems Biomedicine, Department of Pathology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.

FEBS Letters
|April 12, 2019
PubMed
Summary

Tripartite motif (TRIM)14’s PRYSPRY domain has a positively charged surface. This basic interface likely mediates TRIM14’s specific binding to partners with acidic residues, impacting its role against pathogens.

Keywords:
BTN3A1PRYSPRYTRIM14

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Area of Science:

  • Immunology
  • Structural Biology
  • Molecular Biology

Background:

  • Tripartite motif (TRIM)14 is crucial for combating pathogens.
  • Its PRYSPRY domain mediates protein-protein interactions, enabling distinct functions.
  • The structural basis for TRIM14’s binding specificity is currently unknown.

Purpose of the Study:

  • To elucidate the structural basis of TRIM14 PRYSPRY domain’s binding specificity.
  • To identify the molecular determinants responsible for TRIM14’s partner interactions.

Main Methods:

  • X-ray crystallography was used to determine the structure of the TRIM14 PRYSPRY domain.
  • Isothermal titration calorimetry (ITC) was employed to study binding interactions.
  • Bioinformatic analysis of known TRIM14 partners was performed.

Main Results:

  • The crystal structure revealed a distinct positively charged surface on the TRIM14 PRYSPRY domain.
  • ITC experiments demonstrated that the TRIM14 PRYSPRY domain binds to acidic peptides.
  • Analysis of known TRIM14 partners supports the hypothesis of binding to acidic residues.

Conclusions:

  • The PRYSPRY domain of TRIM14 possesses a basic interface potentially responsible for specific interactions.
  • This interface likely binds to partners containing acidic amino acid residues.
  • Understanding this structural basis provides insights into TRIM14's anti-pathogen functions.