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Article

An expanded allosteric network in PTP1B by multitemperature crystallography, fragment screening, and covalent tethering.

eLife - 7 Jun 2018

Keedy Daniel A, Hill Zachary B, Biel Justin T, Kang Emily, Rettenmaier T Justin, Brandão-Neto José, Pearce Nicholas M, von Delft Frank, Wells James A, Fraser James S

Abstract excerpt

Allostery is an inherent feature of proteins, but it remains challenging to reveal the mechanisms by which allosteric signals propagate. A clearer understanding of this intrinsic circuitry would afford new opportunities to modulate protein function. Here, we have identified allosteric sites in protein tyrosine phosphatase 1B (PTP1B) by combining multiple-temperature X-ray crystallography experiments and structure...

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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: 29877794
DOI: 10.7554/eLife.36307
PMCID: PMC6039181

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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