PUBLICATION
Identifying human diamine sensors for death related putrescine and cadaverine molecules
- Authors
- Izquierdo, C., Gómez-Tamayo, J.C., Nebel, J.C., Pardo, L., Gonzalez, A.
- ID
- ZDB-PUB-180622-46
- Date
- 2018
- Source
- PLoS Computational Biology 14: e1005945 (Journal)
- Registered Authors
- Keywords
- none
- MeSH Terms
-
- Animals
- Aspartic Acid/chemistry
- Behavior, Animal
- Cadaverine/chemistry*
- Cell Cycle Proteins/chemistry
- Computational Biology
- Computer Simulation
- Diamines/chemistry*
- Humans
- Ligands
- Molecular Docking Simulation
- Nuclear Proteins/chemistry
- Olfactory Mucosa/physiology
- Phylogeny
- Polyamines/chemistry
- Protein Binding
- Putrescine/chemistry*
- Receptors, G-Protein-Coupled/chemistry
- Smell*
- Zebrafish
- PubMed
- 29324768 Full text @ PLoS Comput. Biol.
Citation
Izquierdo, C., Gómez-Tamayo, J.C., Nebel, J.C., Pardo, L., Gonzalez, A. (2018) Identifying human diamine sensors for death related putrescine and cadaverine molecules. PLoS Computational Biology. 14:e1005945.
Abstract
Pungent chemical compounds originating from decaying tissue are strong drivers of animal behavior. Two of the best-characterized death smell components are putrescine (PUT) and cadaverine (CAD), foul-smelling molecules produced by decarboxylation of amino acids during decomposition. These volatile polyamines act as 'necromones', triggering avoidance or attractive responses, which are fundamental for the survival of a wide range of species. The few studies that have attempted to identify the cognate receptors for these molecules have suggested the involvement of the seven-helix trace amine-associated receptors (TAARs), localized in the olfactory epithelium. However, very little is known about the precise chemosensory receptors that sense these compounds in the majority of organisms and the molecular basis of their interactions. In this work, we have used computational strategies to characterize the binding between PUT and CAD with the TAAR6 and TAAR8 human receptors. Sequence analysis, homology modeling, docking and molecular dynamics studies suggest a tandem of negatively charged aspartates in the binding pocket of these receptors which are likely to be involved in the recognition of these small biogenic diamines.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping