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The structure of the FnI-EGF-like tandem domain of coagulation factor XII solved using SIRAS.

Beringer DX, Kroon-Batenburg LM
Acta Crystallogr Sect F Struct Biol Cryst Commun 69 94-102 (2013)
Cited: 9 times
EuropePMC logo PMID: 23385745

Abstract

Coagulation factor XII (FXII) is a key protein in the intrinsic coagulation and kallikrein-kinin pathways. It has been found that negative surfaces and amyloids, such as Aβ fibrils, can activate FXII. Additionally, it has been suggested that FXII simulates cells and that it plays an important role in thrombosis. To date, no structural data on FXII have been deposited, which makes it difficult to support any hypothesis on the mechanism of FXII function. The crystal structure of the FnI-EGF-like tandem domain of FXII presented here was solved using experimental phases. To determine the phases, a SIRAS approach was used with a native and a holmium chloride-soaked data set. The holmium cluster was coordinated by the C-terminal tails of two symmetry-related molecules. Another observation was that the FnI domain was much more ordered than the EGF-like domain owing to crystal packing. Furthermore, the structure shows the same domain orientation as the homologous FnI-EGF-like tandem domain of tPA. The plausibility of several proposed interactions of these domains of FXII is discussed. Based on this FXII FnI-EGF-like structure, it could be possible that FXII binding to amyloid and negatively charged surfaces is mediated via this part of FXII.

Articles - 4bdw mentioned but not cited (1)

  1. The structure of the FnI-EGF-like tandem domain of coagulation factor XII solved using SIRAS. Beringer DX, Kroon-Batenburg LM. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 69 94-102 (2013)


Articles citing this publication (8)

  1. Coagulation factor XII protease domain crystal structure. Pathak M, Wilmann P, Awford J, Li C, Hamad BK, Fischer PM, Dreveny I, Dekker LV, Emsley J. J. Thromb. Haemost. 13 580-591 (2015)
  2. Heparan sulfate proteoglycans mediate factor XIIa binding to the cell surface. Wujak L, Didiasova M, Zakrzewicz D, Frey H, Schaefer L, Wygrecka M. J. Biol. Chem. 290 7027-7039 (2015)
  3. Molecular characterization of cat factor XII gene and identification of a mutation causing factor XII deficiency in a domestic shorthair cat colony. Bender DE, Kloos MT, Pontius JU, Hinsdale ME, Bellinger DA. Vet. Pathol. 52 312-320 (2015)
  4. A mutation in the kringle domain of human factor XII that causes autoinflammation, disturbs zymogen quiescence, and accelerates activation. Hofman ZLM, Clark CC, Sanrattana W, Nosairi A, Parr NMJ, Živkovic M, Krause K, Mahnke NA, Scheffel J, Hack CE, Maurer M, de Maat S, Maas C. J Biol Chem 295 363-374 (2020)
  5. Factor XII Structure-Function Relationships. Shamanaev A, Litvak M, Ivanov I, Srivastava P, Sun MF, Dickeson SK, Kumar S, He TZ, Gailani D. Semin Thromb Hemost (2023)
  6. Model for surface-dependent factor XII activation: the roles of factor XII heavy chain domains. Shamanaev A, Ivanov I, Sun MF, Litvak M, Srivastava P, Mohammed BM, Shaban R, Maddur A, Verhamme IM, McCarty OJT, Law RHP, Gailani D. Blood Adv 6 3142-3154 (2022)
  7. A site on factor XII required for productive interactions with polyphosphate. Shamanaev A, Litvak M, Cheng Q, Ponczek M, Dickeson SK, Smith SA, Morrissey JH, Gailani D. J Thromb Haemost 21 1567-1579 (2023)
  8. Modeling and dynamical analysis of the full-length structure of factor XII with zinc. Kılınç E, Can Timucin A, Selim Cinaroglu S, Timucin E, Timucin E. J Mol Model 28 129 (2022)


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