Dmitrii V Kalinin: Cryo-EM Reveals Dynamic Conformational Ensemble of Full-Length FXIa
Dmitrii V Kalinin, Lecturer/Assistant Professor at the University of Galway, reposted from University of Galway on LinkedIn:
“Very pleased to share our new preprint on the cryo-EM structures of full-length human Factor XIa.
Our results show that activated FXIa is not a single static structure, but a dynamic ensemble of distinct conformational states.
The observed movement of the catalytic domains provides new insight into FXI activation and reveals potential non-catalytic sites for the future development of selective anticoagulants.
This study was a great collaboration between the University of Münster and the University of Galway.
Many thanks to Alena Siutkina for leading the experimental work and to the entire team for making this study possible!”
Alena Siutkina, Postdoctoral Fellowship University of Münster, shared a post on LinkedIn:
“Factor XIa in motion: How activation reshapes a symmetric homodimer
Coagulation Factor XI is known as a symmetric homodimer, but our new cryoEM structures show that its active form, FXIa, is far from static.
Thanks to cryoEM, we can now see that activated human FXIa is far more dynamic.
I am excited to share our latest research, now available on bioRxiv, conducted in collaboration between the University of Münster and the University of Galway.
In this work, we report cryo-EM structures of full-length human apo-FXIa — the activated enzyme in the absence of bound antibodies, inhibitors, or other ligands.
At the achieved resolution, we could observe:
- A full-length apo-FXIa cryo-EM structure at 2.80 Å resolution
- A major activation-associated repositioning of the catalytic domain relative to the apple-domain platform
- Three distinct apo-FXIa conformational states, revealing pronounced catalytic-domain flexibility
- Molecular dynamics evidence that activation rewires allosteric communication between the two catalytic domains
These findings provide new insight into Factor XIa physiology and highlight potential non-catalytic sites for the future design of more selective FXIa modulators.
Many thanks to the entire team — Alexander Neuhaus, Marvin Taterra, Marcel Bermudez, Christos Gatsogiannis, and Dmitrii Kalinin — as well as George Broutzakis and Dr. Anja Blanque for their valuable support in making this investigation possible.”
Proceed to the video attached to the post.
Stay updated with Hemostasis Today.
-
Sep 8, 2026, 06:51Michael O’Shea: Safety of DOACs Versus Warfarin in Adults with Congenital Heart Disease
-
Sep 8, 2026, 02:49Jared Rice: High Platelets, Low Clot Risk? – What Makes Neonatal Platelets Different in Sepsis
-
Sep 8, 2026, 02:46Rasha E.: Exploring Polycythemia Vera: Beyond the Hematocrit
-
Sep 8, 2026, 02:35Ahmet Davut Aksu: Plasminogen Supplementation Enhances Alteplase Efficacy in Systemic Embolization Model
-
Sep 7, 2026, 23:56Abdel Gaffar Mohammed: Treatment Approaches for Different Types of TMA
-
Sep 7, 2026, 18:36Richard Kollen: Preventing Deep Vein Thrombosis During Long Flights
-
Sep 7, 2026, 18:34Mahmoud Hashem: Apixaban – Doses According to the Reason for Use
-
Sep 7, 2026, 18:31Julian P. Villacastin: LAAC as a Treatment Option When Long-Term Anticoagulation Is Problematic
-
Sep 7, 2026, 18:29Geoff Stooke: How Hemophilia Led the Massie Family to the Romanovs and Ronald Reagan