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

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Figure 7
FXII Zn²⁺-binding sites. (a) Cartoon diagram of the FXII^HC5 structure showing the dimer with the two L-shaped FnII–EGF1–FnI polypeptides, with clusters of surface-exposed histidine residues as potential Zn²⁺-binding sites shown as sticks (cyan). The black dashed line labelled N represents the N-terminus. (b) Cartoon diagram of the isolated FXII^FnII crystal structure with bound Zn²⁺ ions shown as grey spheres. Residue Arg47 is shown in light blue and Pro48 is in green. Other residues are shown as sticks in dark blue. (c) Enlarged view of the His17 and His40 residues shown as sticks, with the coordination sphere of the Zn²⁺ ion (grey sphere) completed by two water molecules (red spheres). Purple dotted lines represent electrostatic interactions formed with Zn²⁺. (d) A charged molecular-surface representation (blue, positive; red, negative) showing the FXII^FnII ABEI domain as a triangular surface of positive charge with two Zn²⁺ ions as grey spheres. Comparison of the FnII domain cation-binding site in the FXII^HC5 crystal structure, where it is occupied by Pro48 (e), compared with the Zn²⁺-bound isolated FXII^FnII (f), where a loop rearrangement occurs and the the Arg47 guanidinium occupies the cation-binding site.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

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

https://doi.org/10.1107/S2059798325005297

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