4NYK

Structure of a membrane protein

Replaces:  3HGC

Summary for 4NYK

• Entry DOI: 10.2210/pdb4nyk/pdb
• Related: 2QTS 3HGC 4FZ0 4NTW 4NTX 4NTY
• Descriptor: Acid-sensing ion channel 1, CHLORIDE ION (3 entities in total)
• Functional Keywords: ion channel, transport protein
• Biological source: Gallus gallus (bantam,chickens)
• Cellular location: Cell membrane; Multi-pass membrane protein (Probable): Q1XA76
• Total number of polymer chains: 1
• Total formula weight: 53587.24

Authors

Baconguis, I.,Bohlen, C.J.,Goehring, A.,Julius, D.,Gouaux, E. (deposition date: 2013-12-10, release date: 2014-02-12)

Primary citation

Gonzales, E.B.,Kawate, T.,Gouaux, E.
Pore architecture and ion sites in acid-sensing ion channels and P2X receptors.
Nature, 460:599-604, 2009

PubMed Abstract: Acid-sensing ion channels are proton-activated, sodium-selective channels composed of three subunits, and are members of the superfamily of epithelial sodium channels, mechanosensitive and FMRF-amide peptide-gated ion channels. These ubiquitous eukaryotic ion channels have essential roles in biological activities as diverse as sodium homeostasis, taste and pain. Despite their crucial roles in biology and their unusual trimeric subunit stoichiometry, there is little knowledge of the structural and chemical principles underlying their ion channel architecture and ion-binding sites. Here we present the structure of a functional acid-sensing ion channel in a desensitized state at 3 A resolution, the location and composition of the approximately 8 A 'thick' desensitization gate, and the trigonal antiprism coordination of caesium ions bound in the extracellular vestibule. Comparison of the acid-sensing ion channel structure with the ATP-gated P2X(4) receptor reveals similarity in pore architecture and aqueous vestibules, suggesting that there are unanticipated yet common structural and mechanistic principles.

PubMed: 19641589
DOI: 10.1038/nature08218

Experimental method

X-RAY DIFFRACTION (3 Å)