Title : Structural insights into transient receptor potential vanilloid type 1 (TRPV1) from homology modeling, flexible docking, and mutational studies.

Pub. Date : 2011 Apr

PMID : 21448716






5 Functional Relationships(s)
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1 We experimentally evaluated by mutational analysis the contribution of residues of rTRPV1 contributing to ligand binding by the prototypical TRPV1 agonists, capsaicin and resiniferatoxin (RTX). resiniferatoxin transient receptor potential cation channel, subfamily V, member 1 Rattus norvegicus
2 We experimentally evaluated by mutational analysis the contribution of residues of rTRPV1 contributing to ligand binding by the prototypical TRPV1 agonists, capsaicin and resiniferatoxin (RTX). resiniferatoxin transient receptor potential cation channel, subfamily V, member 1 Rattus norvegicus
3 We experimentally evaluated by mutational analysis the contribution of residues of rTRPV1 contributing to ligand binding by the prototypical TRPV1 agonists, capsaicin and resiniferatoxin (RTX). resiniferatoxin transient receptor potential cation channel, subfamily V, member 1 Rattus norvegicus
4 We experimentally evaluated by mutational analysis the contribution of residues of rTRPV1 contributing to ligand binding by the prototypical TRPV1 agonists, capsaicin and resiniferatoxin (RTX). resiniferatoxin transient receptor potential cation channel, subfamily V, member 1 Rattus norvegicus
5 Additionally, the binding mode of a simplified RTX (sRTX) ligand as predicted by the modeling agreed well with those of capsaicin and RTX, accounting for the high binding affinity of the sRTX ligand for TRPV1. resiniferatoxin transient receptor potential cation channel, subfamily V, member 1 Rattus norvegicus