Factor XIII topology: organization of B subunits and changes with activation studied with single-molecule atomic force microscopy.

ABSTRACT: Essentials Factor XIII is a heterotetramer with 2 catalytic A subunits and 2 non-catalytic B subunits. Structure of active and inactive factor XIII was studied with atomic force microscopy. Inactive factor XIII is made of an A₂ globule and 2 flexible B subunits extending from it. Activated factor XIII separates into a B₂ homodimer and 2 monomeric active A subunits. SUMMARY: Background Factor XIII (FXIII) is a precursor of the blood plasma transglutaminase (FXIIIa) that is generated by thrombin and Ca²⁺ and covalently crosslinks fibrin to strengthen blood clots. Inactive plasma FXIII is a heterotetramer with two catalytic A subunits and two non-catalytic B subunits. Inactive A subunits have been characterized crystallographically, whereas the atomic structur

SUBMITTER: Protopopova AD 

PROVIDER: S-EPMC6917434 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature