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10.1073/pnas.1700001114 http://scihub22266oqcxt.onion/10.1073/pnas.1700001114 C5347580!5347580 !28228527     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28228527 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Proc+Natl+Acad+Sci+U+S+A 2017 ; 114 (10 ): 2568-2573 Nephropedia Template TP {{tp|p=28228527 |t=2017. Activation mechanism of the G protein-coupled sweet receptor heterodimer with sweeteners and allosteric agonists |pdf=|usr=}}{{28228527 }} gab.com Text Activation mechanism of the G protein-coupled sweet receptor heterodimer with sweeteners and allosteric agonists JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28228527 #FOAvip The sweet taste in humans is mediated by the TAS1R2/TAS1R3 G protein-coupled receptor (GPCR), which belongs to the class C family that also includes the metabotropic glutamate and ?-aminobutyric acid receptors. We report here the predicted 3D structure of the full-length TAS1R2/TAS1R3 heterodimer, including the Venus Flytrap Domains (VFDs) [in the closed-open (co) active conformation], the cysteine-rich domains (CRDs), and the transmembrane domains (TMDs) at the TM56/TM56 interface. We observe that binding of agonists to VFD2 of TAS1R2 leads to major conformational changes to form a TM6/TM6 interface between TMDs of TAS1R2 and TAS1R3, which is consistent with the activation process observed biophysically on the metabotropic glutamate receptor 2 homodimer. We find that the initial effect of the agonist is to pull the bottom part of VFD3/TAS1R3 toward the bottom part of VFD2/TAS1R2 by ?6 Å and that these changes get transmitted from VFD2 of TAS1R2 (where agonists bind) through the VFD3 and the CRD3 to the TMD3 of TAS1R3 (which couples to the G protein). These structural transformations provide a detailed atomistic mechanism for the activation process in GPCR, providing insights and structural details that can now be validated through mutation experiments. Twit Text FOAVip Activation mechanism of the G protein-coupled sweet receptor heterodimer with sweeteners and allosteric agonists ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28228527 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28228527 #FOAvip English Wikipedia <ref>{{Cite pmid|28228527 }}</ref> Activation mechanism of the G protein-coupled sweet receptor heterodimer with sweeteners and allosteric agonists #MMPMID28228527 Kim SK ; Chen Y ; Abrol R ; Goddard WA 3rd ; Guthrie B Proc Natl Acad Sci U S A 2017[Mar]; 114 (10 ): 2568-2573 PMID28228527 show ga The sweet taste in humans is mediated by the TAS1R2/TAS1R3 G protein-coupled receptor (GPCR), which belongs to the class C family that also includes the metabotropic glutamate and ?-aminobutyric acid receptors. We report here the predicted 3D structure of the full-length TAS1R2/TAS1R3 heterodimer, including the Venus Flytrap Domains (VFDs) [in the closed-open (co) active conformation], the cysteine-rich domains (CRDs), and the transmembrane domains (TMDs) at the TM56/TM56 interface. We observe that binding of agonists to VFD2 of TAS1R2 leads to major conformational changes to form a TM6/TM6 interface between TMDs of TAS1R2 and TAS1R3, which is consistent with the activation process observed biophysically on the metabotropic glutamate receptor 2 homodimer. We find that the initial effect of the agonist is to pull the bottom part of VFD3/TAS1R3 toward the bottom part of VFD2/TAS1R2 by ?6 Å and that these changes get transmitted from VFD2 of TAS1R2 (where agonists bind) through the VFD3 and the CRD3 to the TMD3 of TAS1R3 (which couples to the G protein). These structural transformations provide a detailed atomistic mechanism for the activation process in GPCR, providing insights and structural details that can now be validated through mutation experiments. |*Protein Conformation [MESH] |Allosteric Regulation/drug effects [MESH] |Animals [MESH] |Crystallography, X-Ray [MESH] |Humans [MESH] |Mutation [MESH] |Protein Binding [MESH] |Protein Domains [MESH] |Protein Multimerization/genetics [MESH] |Receptors, G-Protein-Coupled/*chemistry/genetics/metabolism [MESH] |Receptors, Metabotropic Glutamate/chemistry [MESH] |Sweetening Agents/chemistry/pharmacology [MESH] |Taste Perception/*genetics [MESH]Activation mechanism of the G protein-coupled sweet receptor heterodim(epmc).pdf DeepDyve Pubget Overpricing