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. Author manuscript; available in PMC: 2017 Jul 18.
Published in final edited form as: J Invest Dermatol. 2016 Sep 3;137(1):142–150. doi: 10.1016/j.jid.2016.08.018

Fig. 2. Electrostatic surface properties of K1-K10-2B.

Fig. 2

(a) K1-K10-2B heterodimer depicted in two orientations, related by 180°, demonstrating the 2B helix has polarization of charge: a mixed acidic and basic character at the N-terminus and predominantly acidic character at the C-terminus. (b) The N-terminal surface of K1-K10-2B is more acidic than the basal keratin complex K5-K14-2B because it contains a glutamate (Glu397K10) rather than lysine (Lys363K14) at homologous positions (circle). The K1-K10 and K5-K14 molecules are structurally aligned in the panel; there are 27 additional N-terminal residues observed in the K1-K10 structure. (c) Acidic patch formed along the N-terminal surface of K10-2B. (d) Acidic pocket formed between Glu397K1 and Glu400K1.