The search result changed since you submitted your search request. Documents might be displayed in a different sort order.
  • search hit 4 of 113
Back to Result List

Extent of intrinsic disorder and NMR chemical shift assignments of the distal N-termini from human TRPV1, TRPV2 and TRPV3 ion channels

  • 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.

Download full text files

Export metadata

Metadaten
Author:Christoph WiedemannORCiDGND, Benedikt GoretzkiORCiDGND, Zoe N. MerzORCiD, Frederike TebbeORCiD, Pauline Schmitt, Ute HellmichORCiDGND
URN:urn:nbn:de:hebis:30:3-694443
DOI:https://doi.org/10.1007/s12104-022-10093-4
ISSN:1874-2718
Parent Title (English):Biomolecular NMR Assignments
Publisher:Springer Netherlands
Place of publication:Dordrecht [u.a.]
Document Type:Article
Language:English
Date of Publication (online):2022/06/06
Date of first Publication:2022/06/06
Publishing Institution:Universitätsbibliothek Johann Christian Senckenberg
Release Date:2023/01/09
Tag:Intrinsically disordered protein; Ion channel; Regulatory domain; Structural dynamics; TRP vanilloid; Transient receptor potential
Volume:16
Issue:2
Page Number:8
First Page:289
Last Page:296
Note:
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.
Note:
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).
Institutes:Wissenschaftliche Zentren und koordinierte Programme / Zentrum für Biomolekulare Magnetische Resonanz (BMRZ)
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 54 Chemie / 540 Chemie und zugeordnete Wissenschaften
5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Sammlungen:Universitätspublikationen
Licence (German):License LogoCreative Commons - CC BY - Namensnennung 4.0 International

OPUS4 Logo