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9ZUB

Structural insights into the exosite-mediated activation of Factor IX by Factor XIa using cryoEM

Summary for 9ZUB
Entry DOI10.2210/pdb9zub/pdb
Related9ZQY 9ZTK
EMDB information74802
DescriptorCoagulation factor XIa heavy chain, Coagulation factor XIa light chain, Coagulation factor IX, ... (5 entities in total)
Functional Keywordscoagulation, intrinsic pathway, complex, hemophilia, factor ix, factor xia, blood clotting
Biological sourceHomo sapiens (human)
More
Total number of polymer chains3
Total formula weight116312.12
Authors
Mohammed, B.M. (deposition date: 2025-12-23, release date: 2026-09-09)
Primary citationMohammed, B.M.,Deavila, S.,Friet, T.,Dattilio, I.
Structural insights into the exosite-mediated activation of Factor IX by Factor XIa using cryo-EM.
J.Thromb.Haemost., 2026
Cited by
PubMed Abstract: Factor XI (FXI) occupies a unique and clinically significant niche, bridging the tissue factor-driven and contact-driven coagulation pathways. Irrespective of the trigger, activated factor XI (FXIa) contributes to clotting by activating factor IX (FIX). Biochemical studies established that this reaction requires the membrane-binding FIX-Gla domain to engage an exosite on the FXIa Apple 3 (A3) domain, that only become available upon FXI activation. Structural data for FXIa, FIX, FIXaβ, and the FXIa:FIX complex are lacking; current understanding relies on zymogen FXI crystal structures and homology modeling of FXIa after kallikrein.
PubMed: 42628751
DOI: 10.1016/j.jtha.2026.08.015
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.65 Å)
Structure validation

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