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Article

Structural basis of allele variation of human thiopurine-S-methyltransferase.

Proteins - 1 Apr 2007

Wu Hong, Horton John R, Battaile Kevin, Allali-Hassani Abdellah, Martin Fernando, Zeng Hong, Loppnau Peter, Vedadi Masoud, Bochkarev Alexey, Plotnikov Alexander N, Cheng Xiaodong

Abstract excerpt

Human thiopurine S-methyltransferase (TPMT) exhibits considerable person-to-person variation in activity to thiopurine drugs. We have produced an N-terminal truncation of human TPMT protein, crystallized the protein in complex with the methyl donor product S-adenosyl-L-homocysteine, and determine...

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Source

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Identifiers

PMID: 17243178
DOI: 10.1002/prot.21272
PMCID: PMC2750861

Genes

TPMT

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-17243178-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

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

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Structural basis of allele variation of human thiopurine-S-methyltransferase.PMID 17243178Read ↗

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