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

. 2014 Jun;143(6):761–782. doi: 10.1085/jgp.201411166

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

© 2014 Keceli and Kubo

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

PMC Copyright notice

Figure 1. — Homology modeling of the structure of rat P2X₂ from zebra fish P2X₄ in closed and open states with localization of the residues K308, D315, and T339S, which are critical in the homotrimer for voltage- and [ATP]–dependent gating. (A and E) Homology model of the rat P2X₂ structure based on the closed- (A) and open-state (E) structures of zebra fish P2X₄ (Kawate et al., 2009; Hattori and Gouaux, 2012). The critical residues at the ATP-binding site (K308), linker (D315), and pore (T339) are shown in pink, magenta, and orange spheres, respectively. (B and F) Only the TM helices and their connections to ATP-binding sites are shown for a better view of critical residues in closed (B) and open (F) states. (C and G) Bottom views of the pore in closed (C) and open (G) states showing T339 residues. (D and H) Top view just above the level of the intersubunit ATP-binding site in closed (D) and open (H) states. K308 and K69 form a groove for the intersubunit ATP docking.