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Updated: Aug 3, 2025

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
Published on: May 26, 2011
Rocking the MBOAT: Structural insights into the membrane bound O-acyltransferase family
Claire E Coupland1, T Bertie Ansell2, Mark S P Sansom3
1Division of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, UK.
Abstract:
The membrane-bound O-acyltransferase (MBOAT) superfamily catalyses the transfer of acyl chains to substrates implicated in essential cellular functions. Aberrant function of MBOATs is associated with various diseases and MBOATs are promising drug targets. There has been recent progress in structural characterisation of MBOATs, advancing our understanding of their functional mechanism. Integrating information across the MBOAT family, we characterise a common MBOAT fold and provide a blueprint for substrate and inhibitor engagement. This work provides context for the diverse substrates, mechanisms, and evolutionary relationships of protein and small-molecule MBOATs. Further work should aim to characterise MBOATs, as inherently lipid-associated proteins, within their membrane environment.
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