TY  - JOUR
A1  - Wiedemann, Christoph
A1  - Goretzki, Benedikt
A1  - Merz, Zoe N.
A1  - Tebbe, Frederike
A1  - Schmitt, Pauline
A1  - Hellmich, Ute
T1  - Extent of intrinsic disorder and NMR chemical shift assignments of the distal N-termini from human TRPV1, TRPV2 and TRPV3 ion channels
T2  - Biomolecular NMR Assignments
N2  - The mammalian Transient Receptor Potential Vanilloid (TRPV) channels are a family of six tetrameric ion channels localized at the plasma membrane. The group I members of the family, TRPV1 through TRPV4, are heat-activated and exhibit remarkable polymodality. The distal N-termini of group I TRPV channels contain large intrinsically disordered regions (IDRs), ranging from ~ 75 amino acids (TRPV2) to ~ 150 amino acids (TRPV4), the vast majority of which is invisible in the structural models published so far. These IDRs provide important binding sites for cytosolic partners, and their deletion is detrimental to channel activity and regulation. Recently, we reported the NMR backbone assignments of the distal TRPV4 N-terminus and noticed some discrepancies between the extent of disorder predicted solely based on protein sequence and from experimentally determined chemical shifts. Thus, for an analysis of the extent of disorder in the distal N-termini of all group I TRPV channels, we now report the NMR assignments for the human TRPV1, TRPV2 and TRPV3 IDRs.
KW  - Transient receptor potential
KW  - TRP vanilloid
KW  - Ion channel
KW  - Intrinsically disordered protein
KW  - Regulatory domain
KW  - Structural dynamics
Y1  - 2022
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/69444
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-694443
SN  - 1874-2718
N1  - Funding
Max Planck Graduate Center PhD Fellowship (to BG), German-American Fulbright Commission (to ZNM), BMRZ funded by the State of Hesse, DFG EXC 2051 – Project ID 390713860.

Open Access funding enabled and organized by Projekt DEAL.
N1  - Availability of data and material
The backbone assignments of the wildtype human TRPV1, TRPV2 and TRPV3 N-terminal intrinsically disordered regions have been deposited in the BioMagResBank (https://bmrb.io) under the accession numbers 51353 (TRPV1-IDR, residues 2-100), 51354 (TRPV2-IDR, residues 2–73) and 51355 (TRPV3-IDR, residues 2-119).
VL  - 16
IS  - 2
SP  - 289
EP  - 296
PB  - Springer Netherlands
CY  - Dordrecht [u.a.]
ER  -