Erythropoietin receptor

From Proteopedia

2 extracellular domains of Human erythropoietin receptor (green) complex with erythropoietin (magenta) (PDB code 1cn4) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Relevance 3 Disease 4 Structural highlights Function Erythropoietin receptor (EpoR) is a 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[1]. See also: Cytokine receptors and Immune receptors Relevance EpoR rescues red blood cells progenitors from apoptosis. Beneficial mutations of EpoR result in increase of red blood cell number and hence better athletic performance. Disease Mutations in EpoR are the cause of erythroleukemia and erythrocytosis. Structural highlights (PDB code 1cn4).[2]

3D Structures of erythropoietin receptor

Updated on 23-February-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
2mxb – EpoR transmembrane domain – mouse - NMR

References

1. ↑ 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
2. ↑ 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