Journal article
Dynamic intraligand binding reveals a new function for PDZ domains
Structure (London), Vol.33(8), pp.1291-1293
08/07/2025
DOI: 10.1016/j.str.2025.07.004
PMCID: PMC12784222
PMID: 40780053
Abstract
PDZ (PSD-95/Discs-large/ZO-1) domains canonically interact with the C termini of partner proteins; however, they also bind internal motifs. In this issue of Structure, Kumar et al.
uncover a novel function of PDZ domains, revealing a dynamic binding mode that alternates between a C-terminal and an internal motif within the same ligand.
Details
- Title: Subtitle
- Dynamic intraligand binding reveals a new function for PDZ domains
- Creators
- Ernesto J Fuentes - University of Iowa
- Resource Type
- Journal article
- Publication Details
- Structure (London), Vol.33(8), pp.1291-1293
- DOI
- 10.1016/j.str.2025.07.004
- PMID
- 40780053
- PMCID
- PMC12784222
- NLM abbreviation
- Structure
- ISSN
- 0969-2126
- eISSN
- 1878-4186
- Publisher
- CELL PRESS
- Grant note
- National Institutes of Health: 1R01AI170557
The work was supported by the National Institutes of Health (grant no. 1R01AI170557 to E.J.F.) . Some elements in Figure 1 were created in BioRender (https:// www.biorender.com /) .
- Language
- English
- Date published
- 08/07/2025
- Academic Unit
- Microbiology and Immunology; Biochemistry and Molecular Biology
- Record Identifier
- 9984945083002771
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