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![[Figure 2]](/d/issues/2025/07/00/gi5044/gi5044fig2mag.jpg)
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| Figure 2 FXIIHC5 intramolecular interactions and charge distribution. (a) Dimer interfacial interactions between the EGF1 and FnI domains are shown with key residues as sticks and electrostatic bonding as purple dotted lines. (b) A charged molecular-surface representation (blue, positive; red, negative) with a continuous flat surface of positive charge generated centrally by the EGF1–FnI domain dimer. Two radial surfaces of further positive charge are generated by the linker and FnII domains. (c) Cartoon diagram showing the dimer with the two L-shaped FnII–EGF1–FnI polypeptides. Clusters of surface-exposed arginine or lysine residues are shown as sticks coloured blue and labelled as anion-binding exosites (ABE). (d) A schematic diagram illustrates the EGF1 and FnI domains with the location of charged residues for ABE2 and ABE3 indicated in the context of the dimer interface (grey). |
![[Figure 2]](https://journals.iucr.org/10.1107/S2059798325005297/gi5044fig2.jpg)
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STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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