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Article

Structure of the catalytic phosphatase domain of MTMR8: implications for dimerization, membrane association and reversible oxidation.

Acta crystallographica. Section D, Biological crystallography - 1 Jul 2015

Yoo Ki Young, Son Ji Young, Lee Jee Un, Shin Woori, Im Dong Won, Kim Seung Jun, Ryu Seong Eon, Heo Yong Seok

Abstract excerpt

Myotubularin-related proteins are a large family of phosphoinositide phosphatases; their activity, stability and subcellular localization are regulated by dimeric interactions with other members of the family. Here, the crystal structure of the phosphatase domain of MTMR8 is reported. Conformational deviation of the two loops that mediate interaction with the PH-GRAM domain suggests that the PH-GRAM domain...

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Topics

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Share to Catalytic Domain
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutagenesis, Site-Directed

Share to Oxidation-Reduction

Share to Phosphatidylinositols

Share to Protein Multimerization

Share to Protein Tyrosine Phosphatases, Non-Receptor

Share to Substrate Specificity

Source

Identifiers

PMID: 26143924
DOI: 10.1107/S139900471500927X

Genes

MTMR8
MTMR2

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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