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10.1016/j.celrep.2016.02.081 http://scihub22266oqcxt.onion/10.1016/j.celrep.2016.02.081 C4902171!4902171!26997265     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26997265&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 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       Cell+Rep 2016 ; 14 (12): 2833-45 Nephropedia Template TP {{tp|p=26997265|t=2016. Structural model of the Extracellular Assembly of the TCR-CD3 Complex |pdf=|usr=}}{{26997265}} gab.com Text Structural model of the Extracellular Assembly of the TCR-CD3 Complex JO: Cell Rep http://www.kidney.de/pget.php?&tw=1&pmid=26997265 #FOAvip Antigen recognition of peptide-major histocompatibility complexes (pMHCs) by T-cells, a key step in initiating adaptive immune responses, is performed by the T-cell receptor (TCR) bound to CD3 heterodimers. However, the biophysical basis of the transmission of TCR-CD3 extracellular interaction into a productive intracellular signaling sequence remains incomplete. Herein, we used nuclear magnetic resonance (NMR) spectroscopy combined with mutational analysis and computational docking to derive a structural model of the extracellular TCR-CD3 assembly. In the inactivated state, CD3?? interacts with the helix-3 and helix 4-F strand regions of the TCR C? subunit while CD3?? interacts with the F and C strand regions of TCR C? subunit in this model, thereby placing the CD3 subunits on opposing sides of the TCR. Together this work identifies the molecular contacts between the TCR and CD3 subunits thereby identifying a physical basis for transmitting an activating signal through the complex. Twit Text FOAVip Structural model of the Extracellular Assembly of the TCR-CD3 Complex ????Cell Rep http://www.kidney.de/pget.php?&tw=1&pmid=26997265 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26997265 #FOAvip English Wikipedia <ref>{{Cite pmid|26997265}}</ref> Structural model of the Extracellular Assembly of the TCR-CD3 Complex #MMPMID26997265 Natarajan A; Nadarajah V; Felsovalyi K; Wang W; Jeyachandran VR; Wasson RA; Cardozo T; Bracken C; Krogsgaard M Cell Rep 2016[Mar]; 14 (12): 2833-45 PMID26997265show ga Antigen recognition of peptide-major histocompatibility complexes (pMHCs) by T-cells, a key step in initiating adaptive immune responses, is performed by the T-cell receptor (TCR) bound to CD3 heterodimers. However, the biophysical basis of the transmission of TCR-CD3 extracellular interaction into a productive intracellular signaling sequence remains incomplete. Herein, we used nuclear magnetic resonance (NMR) spectroscopy combined with mutational analysis and computational docking to derive a structural model of the extracellular TCR-CD3 assembly. In the inactivated state, CD3?? interacts with the helix-3 and helix 4-F strand regions of the TCR C? subunit while CD3?? interacts with the F and C strand regions of TCR C? subunit in this model, thereby placing the CD3 subunits on opposing sides of the TCR. Together this work identifies the molecular contacts between the TCR and CD3 subunits thereby identifying a physical basis for transmitting an activating signal through the complex. äStructural model of the Extracellular Assembly of the TCR-CD3 Complex (epmc).pdf DeepDyve Pubget Overpricing