The TRIM14 PRYSPRY domain mediates protein interaction via its basic interface

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.