Crystal structure of coagulation factor XII N-terminal domains 1–5

Saleem, M.; Li, C.; Kaira, B.G.; Brown, A.K.; Pathak, M.; Najmudin, S.; Cowieson, N.; Dreveny, I.; Wilson, C.; Shamanaev, A.; Gailani, D.; Smith, S.A.; Morrissey, J.H.; Philippou, H.; Emsley, J.

doi:10.1107/S2059798325005297

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 3
FXII^HC5 kringle lysine-binding site. (a) Cartoon diagram of FXII^HC5 in the region of the EGF2 (black) and kringle (red) domains showing the outward-facing lysine-binding sites as sticks engaging the Lys81 side chain (green spheres). (b) Enlarged view of EGF1 Lys81 (green) and the kringle domain lysine-binding site residues shown as sticks. (c) The interface between the EGF1 and the kringle domains involves positive charges on Lys76, Lys81 and His82 from the EGF1 domain coordinating to the kringle domain residues. Electrostatic interactions are shown as purple dotted lines. (d) Kringle-mediated interactions result in three FXII^HC5 dimer forms being arranged into a cyclic hexamer. This hexameric form of the FXII^HC5 structure is represented as a ribbon with the subunits coloured purple, grey, green and yellow and the FnII-less FXII^HC5 dimer coloured cyan and salmon. (e) Two views of the hexameric form of FXII^HC5 shown as a molecular surface.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 81| Part 7| July 2025| Pages 380-393

https://doi.org/10.1107/S2059798325005297

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