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CONFORMATIONAL DYNAMICS LEADING TO ACTIVATION OF THE TRANSGLUTAMINASE FACTOR XIII Richard Tatum Woofter II 16 December 2011 One of the last events that occurs during blood coagulation, a process taken for granted on a daily basis, involves Factor XIII (FXIII) cross-linking fibrin monomers to form an insoluble clot. In plasma, FXIII-A2 is not active and exists as the heterotetramer FXIII-A2B2. Through the utilization of hydrogen deuterium exchange (HDX) coupled with Matrix Assisted Laser Desorption ionization Time of Flight Mass Spectrometry (MALDI-TOF-MS), it was determined that FXIII-A2 becomes nearly uniformly protected when bound to FXIII-B2 and the FXIII-A2 ~-barrels playa major role in heterotetramer formation. After dissociation from FXIII-B2, FXIII-A2 has the ability to become activated in the presence of Ca2+. The regions/residues of FXIII-A2 Ca2+ affects during activation were identified using HDX. It is debated whether FXIII-A2 undergoes an open conformation during activation. Transglutaminase 2 (TG2) has been observed crystallographically in an open conformation. HDX was utilized to compare the conformational dynamics of Transglutaminase 2 in solution to that of FXIII-A2. The increase in exposure between the catalytic core and ~-barrels of TG2 yields evidence of an open conformation. A structural

Conformational dynamics leading to activation of the transglutaminase factor XIII.