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Introducing a New Model of Sweet Taste Receptor, a Class C G-protein Coupled Receptor (C GPCR).

Abstract：

:The structure of sweet taste receptor (STR), a heterodimer of class C G-protein coupled receptors comprising T1R2 and T1R3 molecules, is still undetermined. In this study, a new enhanced model of the receptor is introduced based on the most recent templates. The improvement, stability, and reliability of the model are discussed in details. Each domain of the protein, i.e., VFTM, CR, and TMD, were separately constructed by hybrid-model construction methods and then assembled to build whole monomers. Overall, 680 ns molecular dynamics simulation was performed for the individual domains, the whole monomers and the heterodimer form of the VFTM orthosteric binding site. The latter's structure obtained from 200 ns simulation was docked with aspartame; among various binding sites suggested by FTMAP server, the experimentally suggested binding domain in T1R2 was retrieved. Local three-dimensional structures and helices spans were evaluated and showed acceptable accordance with the template structures and secondary structure predictions. Individual domains and whole monomer structures were found stable and reliable to be used. In conclusion, several validations have shown reliability of the new and enhanced models for further molecular modeling studies on structure and function of STR and C GPCRs.

journal_name

Cell Biochem Biophys

journal_title

Cell biochemistry and biophysics

authors

Kashani-Amin E,Sakhteman A,Larijani B,Ebrahim-Habibi A

doi

10.1007/s12013-019-00872-7

subject

Has Abstract

pub_date

2019-09-01 00:00:00

pages

227-243

issue

3

eissn

1085-9195

issn

1559-0283

pii

10.1007/s12013-019-00872-7

journal_volume

77

pub_type

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