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Article

Probing backbone hydrogen bonding in PDZ/ligand interactions by protein amide-to-ester mutations.

Nature communications - 1 Jan 2014

Pedersen Søren W, Pedersen Stine B, Anker Louise, Hultqvist Greta, Kristensen Anders S, Jemth Per, Strømgaard Kristian

Abstract excerpt

PDZ domains are scaffolding modules in protein-protein interactions that mediate numerous physiological functions by interacting canonically with the C-terminus or non-canonically with an internal motif of protein ligands. A conserved carboxylate-binding site in the PDZ domain facilitates binding via backbone hydrogen bonds; however, little is known about the role of these hydrogen bonds due to experimental...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 24477114
DOI: 10.1038/ncomms4215

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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