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10.7554/eLife.03772 http://scihub22266oqcxt.onion/10.7554/eLife.03772 C4381924!4381924 !25255214     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\25255214 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Elife 2014 ; 3 (ä): ä Nephropedia Template TP {{tp|p=25255214 |t=2014. How IGF-1 activates its receptor |pdf=|usr=}}{{25255214 }} gab.com Text How IGF-1 activates its receptor JO: Elife http://www.kidney.de/pget.php?&tw=1&pmid=25255214 #FOAvip The type I insulin-like growth factor receptor (IGF1R) is involved in growth and survival of normal and neoplastic cells. A ligand-dependent conformational change is thought to regulate IGF1R activity, but the nature of this change is unclear. We point out an underappreciated dimer in the crystal structure of the related Insulin Receptor (IR) with Insulin bound that allows direct comparison with unliganded IR and suggests a mechanism by which ligand regulates IR/IGF1R activity. We test this mechanism in a series of biochemical and biophysical assays and find the IGF1R ectodomain maintains an autoinhibited state in which the TMs are held apart. Ligand binding releases this constraint, allowing TM association and unleashing an intrinsic propensity of the intracellular regions to autophosphorylate. Enzymatic studies of full-length and kinase-containing fragments show phosphorylated IGF1R is fully active independent of ligand and the extracellular-TM regions. The key step triggered by ligand binding is thus autophosphorylation. Twit Text FOAVip How IGF-1 activates its receptor ????Elife http://www.kidney.de/pget.php?&tw=1&pmid=25255214 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25255214 #FOAvip English Wikipedia <ref>{{Cite pmid|25255214 }}</ref> How IGF-1 activates its receptor #MMPMID25255214 Kavran JM ; McCabe JM ; Byrne PO ; Connacher MK ; Wang Z ; Ramek A ; Sarabipour S ; Shan Y ; Shaw DE ; Hristova K ; Cole PA ; Leahy DJ Elife 2014[Sep]; 3 (ä): ä PMID25255214 show ga The type I insulin-like growth factor receptor (IGF1R) is involved in growth and survival of normal and neoplastic cells. A ligand-dependent conformational change is thought to regulate IGF1R activity, but the nature of this change is unclear. We point out an underappreciated dimer in the crystal structure of the related Insulin Receptor (IR) with Insulin bound that allows direct comparison with unliganded IR and suggests a mechanism by which ligand regulates IR/IGF1R activity. We test this mechanism in a series of biochemical and biophysical assays and find the IGF1R ectodomain maintains an autoinhibited state in which the TMs are held apart. Ligand binding releases this constraint, allowing TM association and unleashing an intrinsic propensity of the intracellular regions to autophosphorylate. Enzymatic studies of full-length and kinase-containing fragments show phosphorylated IGF1R is fully active independent of ligand and the extracellular-TM regions. The key step triggered by ligand binding is thus autophosphorylation. |Amino Acid Sequence [MESH] |Animals [MESH] |Conserved Sequence [MESH] |HEK293 Cells [MESH] |Humans [MESH] |Insulin-Like Growth Factor I/*metabolism [MESH] |Ligands [MESH] |Mice [MESH] |Models, Molecular [MESH] |Molecular Sequence Data [MESH] |Mutation/genetics [MESH] |Phosphorylation [MESH] |Protein Binding [MESH] |Protein Multimerization [MESH] |Protein Structure, Tertiary [MESH] |Receptor, IGF Type 1/chemistry/genetics/*metabolism [MESH]How IGF-1 activates its receptor (epmc).pdf DeepDyve Pubget Overpricing