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. 2020 Oct 1;21(19):7280. doi: 10.3390/ijms21197280

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© 2020 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Two-sided view of molecular surfaces of TFPs: (A) trans-Tyr39-Pro40 SLURP-1, (B) cis-Tyr39-Pro40 SLURP-1, (C) Lypd6, (D) Lypd6b, (E) Lynx2, (F) Lynx1, (G) SLURP-2, (H) WTX-P33A, (I) NTII. Electrostatic and molecular hydrophobicity [67] potentials are shown. Red, blue, green, and yellow areas denote negative, positive, polar, and hydrophobic regions, respectively. The ribbon representation shown for each protein/isomer corresponds to the left panel. The predicted glycosylation site (Asn23) in the Lynx2 molecule is shown by asterisk.

Two-sided view of molecular surfaces of TFPs: (A) trans-Tyr39-Pro40 SLURP-1, (B) cis-Tyr39-Pro40 SLURP-1, (C) Lypd6, (D) Lypd6b, (E) Lynx2, (F) Lynx1, (G) SLURP-2, (H) WTX-P33A, (I) NTII. Electrostatic and molecular hydrophobicity [67] potentials are shown. Red, blue, green, and yellow areas denote negative, positive, polar, and hydrophobic regions, respectively. The ribbon representation shown for each protein/isomer corresponds to the left panel. The predicted glycosylation site (Asn23) in the Lynx2 molecule is shown by asterisk.