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TRIM14 was recently shown to be an important molecule against pathogens. Its PRYSPRY domain acts as a protein-protein interaction module. TRIM14 exerts distinct functions via its PRYSPRY domain by interacting with different partners. However, the structural basis for its binding specificity remains unknown. Here we solved the crystal structure of the TRIM14 PRYSPRY domain, and found a positively charged surface that may mediate its partner specificity. Isothermal titration calorimetry (ITC) reveals that the TRIM14 PRYSPRY domain binds to acidic peptides, and the analysis of the reported partners of TRIM14 is consistent with our assumption. Therefore, we demonstrate that the PRYSPRY domain of TRIM14 harbors a putative basic interface that may favorably bind to acidic amino acid residues. This article is protected by copyright. All rights reserved.
This article was published in the following journal.
Name: FEBS letters
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A homodimerization protein interaction domain occurring at the N terminus of proteins that contain multiple copies of either CYS2-HIS2 ZINC FINGERS or KELCH REPEATS. It is characterized by a tightly intertwined dimer with an extensive hydrophobic interface. A surface-exposed groove lined with conserved amino acids is formed at the dimer interface, suggesting a peptide-binding site. Many BTB proteins are transcriptional regulators that are thought to regulate CHROMATIN structure.
A conserved protein interaction domain of the death domain superfamily that is structurally similar to the DEATH EFFECTOR DOMAIN and CASPASE RECRUITMENT DOMAIN. Death domains bind each other to form oligomers and occur on DEATH DOMAIN RECEPTORS, where they are required for APOPTOSIS signaling and non-apoptotic functions.
A homotypic protein interaction module of the death domain superfamily that is composed of a bundle of six alpha-helices. The death effector domain shares sequence and structural similarities with the DEATH DOMAIN and CASPASE RECRUITMENT DOMAIN. It occurs in many proteins with essential functions in APOPTOSIS.
Protein interaction domains of about 70-90 amino acid residues, named after a common structure found in PSD-95, Discs Large, and Zona Occludens 1 proteins. PDZ domains are involved in the recruitment and interaction of proteins, and aid the formation of protein scaffolds and signaling networks. This is achieved by sequence-specific binding between a PDZ domain in one protein and a PDZ motif in another protein.
A subclass of receptor-like protein tryosine phosphatases that contain a short extracellular domain, a cytosolic kinase-interaction domain, and single protein tyrosine kinase domain.
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Collaborations in biotechnology
Commercial and academic collaborations are used throughout the biotechnology and pharmaceutical sector to enhance research and product development. Collaborations can take the form of research and evaluation agreements, licensing, partnerships etc. ...