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10.1016/j.molimm.2003.11.017 http://scihub22266oqcxt.onion/10.1016/j.molimm.2003.11.017 C4515969!4515969!15072848     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       Mol+Immunol 2004 ; 40 (18): 1295-305 Nephropedia Template TP {{tp|p=15072848|t=2004. Molecular mechanisms for the assembly of the T cell receptor?CD3 complex |pdf=|usr=}}{{15072848}} gab.com Text Molecular mechanisms for the assembly of the T cell receptor CD3 complex JO: Mol Immunol http://www.kidney.de/pget.php?&tw=1&pmid=15072848 #FOAvip The T cell receptor (TCR)?CD3 complex represents on of the most intricate membrane receptor structures since it is built from six distinct chains. This complexity led to a number of different proposals for the arrangement of the receptor subunits, its stoichiometry and the mechanisms responsible for receptor triggering. Early work had demonstrated that basic and acidic transmembrane (TM) residues were involved in the assembly but the molecular arrangement could not be deduced due to the complexity of the receptor. Using a novel method for the isolation of intact radiolabeled protein complexes, we demonstrated that the complex assembled in the ER contains only a single TCR?? heterodimer and one copy of each of the CD3??, CD3?? and ??? signaling dimers. Surprisingly, assembly of each of the three signaling dimers with TCR was dependent on one of the three basic TCR TM residues as well as both acidic residues located in the TM domains of the interacting signaling dimer. Each assembly step thus results in the formation of a three-helix interface in the membrane that involves one basic and two acidic TM residues, and this arrangement effectively shields these ionizable residues at protein?protein interfaces from the lipid. Since proteins whose TM domains have exposed ionizable residues are not stably integrated into the lipid bilayer, assembly based on shielding of ionizable residues permits full equilibration of the receptor into the lipid bilayer and prevents degradation. Assembly, export of intact receptor complexes and degradation of unassembled components thus rely on the same organizing principle. Twit Text FOAVip Molecular mechanisms for the assembly of the T cell receptor CD3 complex ????Mol Immunol http://www.kidney.de/pget.php?&tw=1&pmid=15072848 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=15072848 #FOAvip English Wikipedia <ref>{{Cite pmid|15072848}}</ref> Molecular mechanisms for the assembly of the T cell receptor?CD3 complex #MMPMID15072848 Call ME; Wucherpfennig KW Mol Immunol 2004[Apr]; 40 (18): 1295-305 PMID15072848show ga The T cell receptor (TCR)?CD3 complex represents on of the most intricate membrane receptor structures since it is built from six distinct chains. This complexity led to a number of different proposals for the arrangement of the receptor subunits, its stoichiometry and the mechanisms responsible for receptor triggering. Early work had demonstrated that basic and acidic transmembrane (TM) residues were involved in the assembly but the molecular arrangement could not be deduced due to the complexity of the receptor. Using a novel method for the isolation of intact radiolabeled protein complexes, we demonstrated that the complex assembled in the ER contains only a single TCR?? heterodimer and one copy of each of the CD3??, CD3?? and ??? signaling dimers. Surprisingly, assembly of each of the three signaling dimers with TCR was dependent on one of the three basic TCR TM residues as well as both acidic residues located in the TM domains of the interacting signaling dimer. Each assembly step thus results in the formation of a three-helix interface in the membrane that involves one basic and two acidic TM residues, and this arrangement effectively shields these ionizable residues at protein?protein interfaces from the lipid. Since proteins whose TM domains have exposed ionizable residues are not stably integrated into the lipid bilayer, assembly based on shielding of ionizable residues permits full equilibration of the receptor into the lipid bilayer and prevents degradation. Assembly, export of intact receptor complexes and degradation of unassembled components thus rely on the same organizing principle. äMolecular mechanisms for the assembly of the T cell receptor?CD3 compl(epmc).pdf DeepDyve Pubget Overpricing