Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2022 Aug 2;609(7927):611–615. doi: 10.1038/s41586-022-05143-9

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2022

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Extended Data Fig. 5 — a, The first and last five TMs of PIN1 are structurally inverted repeats. TM6-10 merges well with TM1-5 by two rotational operations as indicated. b, The dimer interface of PIN1 is formed by TM1, 2, 7 of each monomer. c, The dimer interface mainly consists of hydrophobic residues. d, Two sodium binding sites of ASBT_NM (left) and the corresponding positions in the Na⁺/H⁺ transporter NapA (right). Left, the sodium ions are shown in purple spheres. N265 and the substrate taurocholate are shown in sticks. The water molecule mediating the interaction between N265 and taurocholate is shown in a red sphere. Right, a lysine residue is present in the Na1 site in NapA and stabilizes the crossover helices through ionic interactions. The Na2 site of NapA is composed of mainly hydrophobic residues as shown in sticks. e, Structural alignments between PIN1 and the inward-facing structures of ASBT_YF (PDB code: 4N7W) and ASBT_NM (PDB code: 3ZUX).