5HI9

Structure of the full-length TRPV2 channel by cryo-electron microscopy

Summary for 5HI9

• Entry DOI: 10.2210/pdb5hi9/pdb
• EMDB information: 6580 6618
• Descriptor: Transient Receptor Potential Cation Channel Subfamily V Member 2 (1 entity in total)
• Functional Keywords: trpv2 ion channel, transport protein
• Biological source: Rattus norvegicus
• Cellular location: Cell membrane; Multi-pass membrane protein: Q9WUD2
• Total number of polymer chains: 4
• Total formula weight: 350671.16

Authors

Huynh, K.W.,Cohen, M.R.,Jiansen, J.,Samanta, A.,Lodowski, D.T.,Zhou, Z.H.,Moiseenkova-Bell, V.Y. (deposition date: 2016-01-11, release date: 2016-03-30, Last modification date: 2024-03-06)

Primary citation

Huynh, K.W.,Cohen, M.R.,Jiang, J.,Samanta, A.,Lodowski, D.T.,Zhou, Z.H.,Moiseenkova-Bell, V.Y.
Structure of the full-length TRPV2 channel by cryo-EM.
Nat Commun, 7:11130-11130, 2016

PubMed Abstract: Transient receptor potential (TRP) proteins form a superfamily Ca(2+)-permeable cation channels regulated by a range of chemical and physical stimuli. Structural analysis of a 'minimal' TRP vanilloid subtype 1 (TRPV1) elucidated a mechanism of channel activation by agonists through changes in its outer pore region. Though homologous to TRPV1, other TRPV channels (TRPV2-6) are insensitive to TRPV1 activators including heat and vanilloids. To further understand the structural basis of TRPV channel function, we determined the structure of full-length TRPV2 at ∼5 Å resolution by cryo-electron microscopy. Like TRPV1, TRPV2 contains two constrictions, one each in the pore-forming upper and lower gates. The agonist-free full-length TRPV2 has wider upper and lower gates compared with closed and agonist-activated TRPV1. We propose these newly revealed TRPV2 structural features contribute to diversity of TRPV channels.

PubMed: 27021073
DOI: 10.1038/ncomms11130

Experimental method

ELECTRON MICROSCOPY (4.4 Å)