Erythropoietin receptor
From Proteopedia
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'''Erythropoietin receptor''' (EpoR) is a [[Cytokine receptors|cytokine receptor]]. Upon binding of erythropoietin (Epo), EpoR changes from a monomer to a dimer. This change induces the activation of Jak2 kinase via its autophophorylation. Specific tyrosines in the intracellular part of EpoR are phosphorylated and activate various cascades of signal transduction which lead to the formation and maturation of red blood cells<ref>PMID:8481505</ref>. | '''Erythropoietin receptor''' (EpoR) is a [[Cytokine receptors|cytokine receptor]]. Upon binding of erythropoietin (Epo), EpoR changes from a monomer to a dimer. This change induces the activation of Jak2 kinase via its autophophorylation. Specific tyrosines in the intracellular part of EpoR are phosphorylated and activate various cascades of signal transduction which lead to the formation and maturation of red blood cells<ref>PMID:8481505</ref>. | ||
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| + | See also: [[Cytokine receptors]]. | ||
== Relevance == | == Relevance == | ||
Revision as of 09:35, 9 January 2023
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3D Structures of erythropoietin receptor
Updated on 09-January-2023
1ern – hEpoR extracellular domain 25-249 - human
2mv6 – hEpoR transmembrane domain 237-284 - NMR
1ebp, 1eba – hEpoR extracellular domain + Epo peptide
1cn4, 1eer – hEpoR extracellular domain (mutant) + Epo (mutant)
2jix – hEpoR extracellular domain + antibody
4y5x, 4y5v, 4y5y – hEpoR extracellular domain + diabody
6moe, 6moh, 6moj, 6mof, 6moi, 6mok, 6mol – hEpoR extracellular domain + darpin
6mol, 6e2q – hEpoR residues 273-338 + JAK2
References
- ↑ Youssoufian H, Longmore G, Neumann D, Yoshimura A, Lodish HF. Structure, function, and activation of the erythropoietin receptor. Blood. 1993 May 1;81(9):2223-36. PMID:8481505
- ↑ Syed RS, Reid SW, Li C, Cheetham JC, Aoki KH, Liu B, Zhan H, Osslund TD, Chirino AJ, Zhang J, Finer-Moore J, Elliott S, Sitney K, Katz BA, Matthews DJ, Wendoloski JJ, Egrie J, Stroud RM. Efficiency of signalling through cytokine receptors depends critically on receptor orientation. Nature. 1998 Oct 1;395(6701):511-6. PMID:9774108 doi:http://dx.doi.org/10.1038/26773

