Jacinto López Sagaseta: Solving the Structural Puzzle of FVIIa–EPCR Interaction
Jacinto López Sagaseta, Unit of Protein Crystallography and Structural Immunology-Navarrabiomed, shared a post on LinkedIn about a recent article he and his colleagues co-authored published in Blood Advances, adding:
“Recombinant factor VIIa (rFVIIa) is an important clinical intervention for severe bleeding, but some aspects associated with its mechanism of action have remained unresolved.
In 2007, several groups reported that FVIIa directly binds EPCR, an endothelial receptor, with consequences for the hemostatic effect of rFVIIa.
Despite extensive investigation, the structural basis of this interaction had remained elusive.
In this work, we report the experimental structure of the FVIIa Gla domain bound to EPCR, providing a missing structural piece in the study of FVIIa.
This is a particularly intricate protein complex, as it involves several residues of y-carboxyglutamate-an unusual yet naturally occurring amino acid, divalent ions, and a phospholipid molecule.
As such, it may also represent an interesting case for AI-based protein structure prediction and associated computational resources.
We are pleased to place this work in the context of the earlier study (2002) by Ogannesyan et al, who solved the structure of the protein C Gla domain bound to the same receptor, a landmark contribution to the structural biology of coagulation.
We would also like to thank the staff of the Xaira and Xaloc beamlines at the ALBA Synchrotron.
Further details can be found in the publication.”
Title: Structure of factor VII Gla domain bound to EPCR
Authors: Jacinto López-Sagaseta, María Gilda, Dichiara-Rodríguez
Title: The Crystal Structure of the Endothelial Protein C Receptor and a Bound Phospholipid
Authors: Vaheh Oganesyan, Natalia Oganesyan, Simon Terzyan, Zbigniew Dauter, Naomi L. Esmon, Charles T. Esmon
Read the Full Article on The Journal of Biological Chemistry
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