This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


Erythropoietin

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 15: Line 15:
'''Structure'''.
'''Structure'''.
-
The gene for EPO is found on chromosome 7 and is composed of five exons and four introns <ref>PMID: 1557429</ref>. The transcriptional product of this gene is an amino acid chain of 193 bases. During translation, the chain is modified to 166 amino acids <ref>PMID:17253966</ref>. The cleaved 27 amino acid leader sequence is made mostly of hydrophobic amino acids. After translation is complete, the C-terminus loses its final arginine residue to reach its final length of 165 amino acids residues <ref>DOI 10.1007/BF02934992</ref>. The total glycoprotein weighs 30 kDa with the peptide backbone weighing 18 kDa. EPO is a glycoprotein composed of only <scene name='12/128258/Epoalpha/1'>Alpha Helices</scene> <ref>DOI 10.1007/BF02934992</ref>. The sulfur of the cysteine residues links to form disulfide bonds. These disulfide bonds help keep EPO's structure. Helix A is connected to Helix D by <scene name='58/583377/Epocyslabels/1'>Cys7 and Cys161</scene>, while Helix A and Helix B are connected by <scene name='58/583377/Epocyslabels/1'>Cys29 and Cys33</scene> . EPO’s structure was determined in 1993. It is made up of four alpha helixes. EPO is produced mainly in the kidney, but further research has shown the brain and liver still produce small amounts <ref>DOI 10.1007/BF02934992</ref>.
+
The gene for EPO is found on chromosome 7 and is composed of five exons and four introns <ref>PMID: 1557429</ref>. The transcriptional product of this gene is an amino acid chain of 193 bases. During translation, the chain is modified to 166 amino acids <ref>PMID:17253966</ref>. The cleaved 27 amino acid leader sequence is made mostly of hydrophobic amino acids. After translation is complete, the C-terminus loses its final arginine residue to reach its final length of 165 amino acids residues <ref> Erslev, A. J., and J. Caro. "Physiologic and molecular biology of erythropoietin." Medical oncology and tumor pharmacotherapy 3.3-4 (1986): 159-164. </ref>. The total glycoprotein weighs 30 kDa with the peptide backbone weighing 18 kDa. EPO is a glycoprotein composed of only <scene name='12/128258/Epoalpha/1'>Alpha Helices</scene> <ref>Erslev, A. J., and J. Caro. "Physiologic and molecular biology of erythropoietin." Medical oncology and tumor pharmacotherapy 3.3-4 (1986): 159-164.</ref>. The sulfur of the cysteine residues links to form disulfide bonds. These disulfide bonds help keep EPO's structure. Helix A is connected to Helix D by <scene name='58/583377/Epocyslabels/1'>Cys7 and Cys161</scene>, while Helix A and Helix B are connected by <scene name='58/583377/Epocyslabels/1'>Cys29 and Cys33</scene> . EPO’s structure was determined in 1993. It is made up of four alpha helixes. EPO is produced mainly in the kidney, but further research has shown the brain and liver still produce small amounts <ref> Erslev, A. J., and J. Caro. "Physiologic and molecular biology of erythropoietin." Medical oncology and tumor pharmacotherapy 3.3-4 (1986): 159-164.</ref>.
'''Stimulus'''
'''Stimulus'''

Revision as of 20:10, 24 April 2014

Erythropoietin Structure, Function, and History

PDB ID 1buy

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

Marie Walsh, Michal Harel, Alexander Berchansky, Ann Taylor

Retrieved from "http://52.214.119.220/wiki/index.php/Erythropoietin"
Personal tools