Full metadata
Title
Probing TRPV1 Polymodal Activation: A Study of the Human TRPV1 Voltage-Sensing Like Domain
Description
Transient Receptor Potential Vanilloid-1 (TRPV1) is an integral membrane polymodal cation channel involved in various essential biological functions, including thermosensing, thermoregulation, and nociception. Discrete TRPV1 activation modes such as ligand, heat, and proton have been challenging to disentangle. However, dissecting the polymodal nature of TRPV1 is essential for therapeutic development. The human TRPV1 (hTRPV1) voltage-sensing like domain (VSLD; transmembrane helices S1-S4) contains the canonical vanilloid ligand binding site and significantly contributes to thermosensing. Nuclear magnetic resonance (NMR)-detected studies probe the role of the hTRPV1-VSLD in TRPV1 polymodal function. The hTRPV1-VSLD is identified as an allosteric hub for all three primary TRPV1 activation modes and demonstrates plasticity in chemical ligand modulation. The presented results underscore molecular features in the VSLD that dictate TRPV1 function, highlighting important considerations for future therapeutic design.
Date Created
2023
Contributors
- Owens, Aerial M. (Author)
- Van Horn, Wade D. (Thesis advisor)
- Levitus, Marcia (Committee member)
- LaBaer, Joshua (Committee member)
- Arizona State University (Publisher)
Topical Subject
Resource Type
Extent
299 pages
Language
eng
Copyright Statement
In Copyright
Primary Member of
Peer-reviewed
No
Open Access
No
Handle
https://hdl.handle.net/2286/R.2.N.190763
Level of coding
minimal
Cataloging Standards
Note
Partial requirement for: Ph.D., Arizona State University, 2023
Field of study: Natural Science
System Created
- 2023-12-14 01:16:26
System Modified
- 2023-12-14 01:16:31
- 11 months 1 week ago
Additional Formats