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Article

Human thymidylate synthase with loop 181-197 stabilized in an inactive conformation: ligand interactions, phosphorylation, and inhibition profiles.

Protein science : a publication of the Protein Society - 1 Jan 2011

Luo BeiBei, Repalli Jayanthi, Yousef Al-Motassem, Johnson Saphronia R, Lebioda Lukasz, Berger Sondra H

Abstract excerpt

Thymidylate synthase (TS) is a well-validated cancer target that undergoes conformational switching between active and inactive states. Two mutant human TS (hTS) proteins are predicted from crystal structures to be stabilized in an inactive conformation to differing extents, with M190K populating...

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Identifiers

PMID: 21064161
DOI: 10.1002/pro.539
PMCID: PMC3047064

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-21064161-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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