COMPLETE CITATION
Citation and identifiers
An S, Yeo KJ, Jeon YH, Song JJ. “Crystal structure of the human histone methyltransferase ASH1L catalytic domain and its implications for the regulatory mechanism.” Journal of Biological Chemistry. 286(10):8369–8374 · doi:10.1074/jbc.M110.203380.
- PubMed ID
- 21239497 ↗
RESEARCH QUESTION
What structural feature of the human ASH1L catalytic domain explains its autoinhibited state?
The catalytic-domain crystal structure identifies a substrate-blocking autoinhibitory loop but cannot assign cell-type effects or the consequences of clinical variants.
INTERPRETATION BOUNDARY
Read the finding and limit together.
What this study supports
Foundational catalytic-domain structure demonstrating an autoinhibitory loop that blocks substrate access in the inactive state.
What it cannot establish
Purified catalytic-domain structure does not define cell-type phenotype or clinical variant effect.
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