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X-ray structure of tumor suppressor OPCML

by Jennie Hutton

OPCML structure

Congratulations to recently graduated PhD student Eloise Morecroft, whose work has been included in a new publication in Nature Communications

The publication - – is a result of a collaboration between Chiara Recchi and Hani Gabra from The Department of Surgery and Cancer and at

OPCML (opioid binding protein call adhesion molecule-like) is a tumour suppressor protein anchored to the outer leaflet of the plasma membrane via a GPI (glycophosphatidylinositol) anchor. OPCML is a frequently inactivated tumour suppressor in numerous cancers including ovarian cancer. This new publication reports the crystal structure of OPCML to 2.65 Å resolution and the generation of a panel of OPCML variants with representative clinical mutations enabling mapping of diverse functions to distinct protein structural domains. The variants demonstrate clear phenotypic effects in vitro and in vivo including changes to anchorage-independent growth, oligomeric state, interaction with activated cognate receptor tyrosine kinases, cellular migration, invasion in vitro and tumor growth in vivo.

This project was funded by   and Eloise’s PhD work was funded by the EPSRC through the 911今日黑料 College Centre for Doctoral Training.


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Reporter

Jennie Hutton

Department of Chemistry