LITERATURE · PEER REVIEWED

Structural insights into stimulation of Ash1L's H3K36 methyltransferase activity through Mrg15 binding

Structure · 2019 · Peer reviewed

COMPLETE CITATION

Citation and identifiers

Hou P, Lee JS, Zhao R, et al.. “Structural insights into stimulation of Ash1L's H3K36 methyltransferase activity through Mrg15 binding.” Structure. 27(5):837–845.e3 · doi:10.1016/j.str.2019.01.015.

PubMed ID
30827843

RESEARCH QUESTION

What structural features explain stimulation of Ash1L H3K36 methyltransferase activity through Mrg15 binding?

This structural analysis defines the Mrg15-associated activation architecture of the catalytic region without functioning as a clinical phenotype or variant-severity assay.

INTERPRETATION BOUNDARY

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What this study supports

Defines MRG15-associated activation and the autoinhibitory architecture of the ASH1L catalytic region.

What it cannot establish

Structural complex evidence is not a clinical phenotype or variant-severity assay.

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