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10.1126/sciadv.abg8685 http://scihub22266oqcxt.onion/10.1126/sciadv.abg8685 34134983!8208711!34134983     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Sci+Adv 2021 ; 7 (25): ä Nephropedia Template TP {{tp|p=34134983|t=2021. Structural basis of the activation of the CC chemokine receptor 5 by a chemokine agonist |pdf=|usr=}}{{34134983}} gab.com Text Structural basis of the activation of the CC chemokine receptor 5 by a chemokine agonist JO: Sci Adv http://www.kidney.de/pget.php?&tw=1&pmid=34134983 #FOAvip The human CC chemokine receptor 5 (CCR5) is a G protein-coupled receptor (GPCR) that plays a major role in inflammation and is involved in cancer, HIV, and COVID-19. Despite its importance as a drug target, the molecular activation mechanism of CCR5, i.e., how chemokine agonists transduce the activation signal through the receptor, is yet unknown. Here, we report the cryo-EM structure of wild-type CCR5 in an active conformation bound to the chemokine super-agonist [6P4]CCL5 and the heterotrimeric G(i) protein. The structure provides the rationale for the sequence-activity relation of agonist and antagonist chemokines. The N terminus of agonist chemokines pushes onto specific structural motifs at the bottom of the orthosteric pocket that activate the canonical GPCR microswitch network. This activation mechanism differs substantially from other CC chemokine receptors that bind chemokines with shorter N termini in a shallow binding mode involving unique sequence signatures and a specialized activation mechanism. Twit Text FOAVip Structural basis of the activation of the CC chemokine receptor 5 by a chemokine agonist ????Sci Adv http://www.kidney.de/pget.php?&tw=1&pmid=34134983 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34134983 #FOAvip English Wikipedia <ref>{{Cite pmid|34134983}}</ref> Structural basis of the activation of the CC chemokine receptor 5 by a chemokine agonist #MMPMID34134983 Isaikina P; Tsai CJ; Dietz N; Pamula F; Grahl A; Goldie KN; Guixa-Gonzalez R; Branco C; Paolini-Bertrand M; Calo N; Cerini F; Schertler GFX; Hartley O; Stahlberg H; Maier T; Deupi X; Grzesiek S Sci Adv 2021[Jun]; 7 (25): ä PMID34134983show ga The human CC chemokine receptor 5 (CCR5) is a G protein-coupled receptor (GPCR) that plays a major role in inflammation and is involved in cancer, HIV, and COVID-19. Despite its importance as a drug target, the molecular activation mechanism of CCR5, i.e., how chemokine agonists transduce the activation signal through the receptor, is yet unknown. Here, we report the cryo-EM structure of wild-type CCR5 in an active conformation bound to the chemokine super-agonist [6P4]CCL5 and the heterotrimeric G(i) protein. The structure provides the rationale for the sequence-activity relation of agonist and antagonist chemokines. The N terminus of agonist chemokines pushes onto specific structural motifs at the bottom of the orthosteric pocket that activate the canonical GPCR microswitch network. This activation mechanism differs substantially from other CC chemokine receptors that bind chemokines with shorter N termini in a shallow binding mode involving unique sequence signatures and a specialized activation mechanism. |Chemokine CCL5/chemistry/metabolism[MESH] |Cryoelectron Microscopy[MESH] |Humans[MESH] |Models, Molecular[MESH] |Molecular Dynamics Simulation[MESH] |Protein Conformation[MESH] |Receptors, CCR5/agonists/*chemistry/genetics/*metabolism[MESH] |Signal Transduction[MESH]Structural basis of the activation of the CC chemokine receptor 5 by a(epmc).pdf DeepDyve Pubget Overpricing