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000145024 0247_ $$2doi$$a10.3390/biom9120765
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000145024 041__ $$aEnglish
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000145024 1001_ $$aSingh, Sneha$$b0
000145024 245__ $$aThe Plasma Factor XIII Heterotetrameric Complex Structure: Unexpected Unequal Pairing within a Symmetric Complex.
000145024 260__ $$aBasel$$bMDPI$$c2019
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000145024 520__ $$aFactor XIII (FXIII) is a predominant determinant of clot stability, strength, and composition. Plasma FXIII circulates as a pro-transglutaminase with two catalytic A subunits and two carrier-protective B subunits in a heterotetramer (FXIII-A2B2). FXIII-A2 and -B2 subunits are synthesized separately and then assembled in plasma. Following proteolytic activation by thrombin and calcium-mediated dissociation of the B subunits, activated FXIII (FXIIIa) covalently cross links fibrin, promoting clot stability. The zymogen and active states of the FXIII-A subunits have been structurally characterized; however, the structure of FXIII-B subunits and the FXIII-A2B2 complex have remained elusive. Using integrative hybrid approaches including atomic force microscopy, cross-linking mass spectrometry, and computational approaches, we have constructed the first all-atom model of the FXIII-A2B2 complex. We also used molecular dynamics simulations in combination with isothermal titration calorimetry to characterize FXIII-A2B2 assembly, activation, and dissociation. Our data reveal unequal pairing of individual subunit monomers in an otherwise symmetric complex, and suggest this unusual structure is critical for both assembly and activation of this complex. Our findings enhance understanding of mechanisms associating FXIII-A2B2 mutations with disease and have important implications for the rational design of molecules to alter FXIII assembly or activity to reduce bleeding and thrombotic complications.
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000145024 650_2 $$2MeSH$$aCalcium: pharmacology
000145024 650_2 $$2MeSH$$aFactor XIII: chemistry
000145024 650_2 $$2MeSH$$aHEK293 Cells
000145024 650_2 $$2MeSH$$aHumans
000145024 650_2 $$2MeSH$$aMolecular Docking Simulation
000145024 650_2 $$2MeSH$$aProtein Conformation
000145024 650_2 $$2MeSH$$aProtein Multimerization
000145024 650_2 $$2MeSH$$aProtein Subunits: chemistry
000145024 650_2 $$2MeSH$$aThermodynamics
000145024 650_2 $$2MeSH$$aThrombin: pharmacology
000145024 7001_ $$aNazabal, Alexis$$b1
000145024 7001_ $$0P:(DE-2719)2812350$$aKaniyappan, Senthilvelrajan$$b2$$udzne
000145024 7001_ $$aPellequer, Jean-Luc$$b3
000145024 7001_ $$aWolberg, Alisa S$$b4
000145024 7001_ $$aImhof, Diana$$b5
000145024 7001_ $$aOldenburg, Johannes$$b6
000145024 7001_ $$0P:(DE-HGF)0$$aBiswas, Arijit$$b7$$eCorresponding author
000145024 77318 $$2Crossref$$3journal-article$$a10.3390/biom9120765$$b : MDPI AG, 2019-11-21$$n12$$p765$$tBiomolecules$$v9$$x2218-273X$$y2019
000145024 773__ $$0PERI:(DE-600)2701262-1$$a10.3390/biom9120765$$gVol. 9, no. 12, p. 765 -$$n12$$p765$$tBiomolecules$$v9$$x2218-273X$$y2019
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