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Article

Real-time observation of ligand-induced allosteric transitions in a PDZ domain.

Proceedings of the National Academy of Sciences of the United States of America - 20 Oct 2020

Bozovic Olga, Zanobini Claudio, Gulzar Adnan, Jankovic Brankica, Buhrke David, Post Matthias, Wolf Steffen, Stock Gerhard, Hamm Peter

Abstract excerpt

While allostery is of paramount importance for protein regulation, the underlying dynamical process of ligand (un)binding at one site, resulting time evolution of the protein structure, and change of the binding affinity at a remote site are not well understood. Here the ligand-induced conformational transition in a widely studied model system of allostery, the PDZ2 domain, is investigated by transient infrared...

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Share to Allosteric Regulation
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 33020277
DOI: 10.1073/pnas.2012999117
PMCID: PMC7585012

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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