 |
PDBsum entry 2n27
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Metal binding protein
|
PDB id
|
|
|
|
2n27
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Metal binding protein
|
|
|
Title:
|
|
Competitive inhibition of trpv1 calmodulin interaction by vanilloids
|
|
Structure:
|
|
Calmodulin. Chain: a. Fragment: unp residues 2-149. Synonym: cam. Engineered: yes
|
|
Source:
|
|
Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
NMR struc:
|
|
20 models
|
|
|
Authors:
|
|
A.Hetenyi,L.Nemeth,E.Weber,G.Szakonyi,Z.Winter,K.Josvay,E.Bartus, Z.Olah,T.A.Martinek
|
|
Key ref:
|
|
A.Hetényi
et al.
(2016).
Competitive inhibition of TRPV1-calmodulin interaction by vanilloids.
Febs Lett,
590,
2768-2775.
PubMed id:
DOI:
|
|
|
Date:
|
|
|
29-Apr-15
|
Release date:
|
06-Jul-16
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
P0DP23
(CALM1_HUMAN) -
Calmodulin-1 from Homo sapiens
|
|
|
|
Seq:
Struc:
|
|
|
|
149 a.a.
148 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
 |
PfamA domain |
|
|
 |
Secondary structure |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
DOI no:
|
Febs Lett
590:2768-2775
(2016)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Competitive inhibition of TRPV1-calmodulin interaction by vanilloids.
|
|
A.Hetényi,
L.Németh,
E.Wéber,
G.Szakonyi,
Z.Winter,
K.Jósvay,
Ã.‰.Bartus,
Z.Oláh,
T.A.Martinek.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
There is enormous interest toward vanilloid agonists of the pain receptor TRPV1
in analgesic therapy, but the mechanisms of their sensory neuron-blocking
effects at high or repeated doses are still a matter of debate. Our results have
demonstrated that capsaicin and resiniferatoxin form nanomolar complexes with
calmodulin, and competitively inhibit TRPV1-calmodulin interaction. These
interactions involve the protein recognition interface of calmodulin, which is
responsible for all of the cell-regulatory calmodulin-protein interactions.
These results draw attention to a previously unknown vanilloid target, which may
contribute to the explanation of the paradoxical pain-modulating behavior of
these important pharmacons.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Links
