6L93

X-ray structure of the ligand-free human TRPV1 ankyrin repeat domain

Summary for 6L93

• Entry DOI: 10.2210/pdb6l93/pdb
• Descriptor: Transient receptor potential cation channel subfamily V member 1 (1 entity in total)
• Functional Keywords: channel domain, transport protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 6
• Total formula weight: 184998.86

Authors

Tanaka, M.,Hayakawa, K.,Unno, M. (deposition date: 2019-11-08, release date: 2020-03-18, Last modification date: 2023-11-22)

Primary citation

Tanaka, M.,Hayakawa, K.,Ogawa, N.,Kurokawa, T.,Kitanishi, K.,Ite, K.,Matsui, T.,Mori, Y.,Unno, M.
Structure determination of the human TRPV1 ankyrin-repeat domain under nonreducing conditions.
Acta Crystallogr.,Sect.F, 76:130-137, 2020

PubMed Abstract: TRPV1, a member of the transient receptor potential (TRP) channels family, has been found to be involved in redox sensing. The crystal structure of the human TRPV1 ankyrin-repeat domain (TRPV1-ARD) was determined at 4.5 Å resolution under nonreducing conditions. This is the first report of the crystal structure of a ligand-free form of TRPV1-ARD and in particular of the human homologue. The structure showed a unique conformation in finger loop 3 near Cys258, which is most likely to be involved in inter-subunit disulfide-bond formation. Also, in human TRPV1-ARD it was possible for solvent to access Cys258. This structural feature might be related to the high sensitivity of human TRPV1 to oxidants. ESI-MS revealed that Cys258 did not form an S-OH functionality even under nonreducing conditions.

PubMed: 32133998
DOI: 10.1107/S2053230X20001533

Experimental method

X-RAY DIFFRACTION (4.47 Å)