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Article

Conformational Rigidity and Protein Dynamics at Distinct Timescales Regulate PTP1B Activity and Allostery.

Molecular cell - 16 Feb 2017

Choy Meng S, Li Yang, Machado Luciana E S F, Kunze Micha B A, Connors Christopher R, Wei Xingyu, Lindorff-Larsen Kresten, Page Rebecca, Peti Wolfgang

Abstract excerpt

Protein function originates from a cooperation of structural rigidity, dynamics at different timescales, and allostery. However, how these three pillars of protein function are integrated is still only poorly understood. Here we show how these pillars are connected in Protein Tyrosine Phosphatase 1B (PTP1B), a drug target for diabetes and cancer that catalyzes the dephosphorylation of numerous substrates in...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Nuclear Magnetic Resonance, Biomolecular

Share to Protein Conformation, alpha-Helical

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Share to Protein Tyrosine Phosphatase, Non-Receptor Type 1

Source

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Identifiers

PMID: 28212750
DOI: 10.1016/j.molcel.2017.01.014
PMCID: PMC5325675

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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