User:Gourinchas Geoffrey/Sandbox 205
From Proteopedia
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== Structure == | == Structure == | ||
| - | <StructureSection load='1buy' size='500' side='right' caption='Structure Erythropoietin (PDB entry [[1buy]])' scene='User:Gourinchas_Geoffrey/Sandbox_205/Photo_of_the_structure/1'> | + | <StructureSection load='1buy' size='500' side='right' caption='Structure Erythropoietin (PDB entry [[1buy]])' scene='User:Gourinchas_Geoffrey/Sandbox_205/Photo_of_the_structure/1'></scene>'> This hormone weight 30.4kD and is constituted to 166 amino acids. |
It is composed to 4 alpha-helix: αA, αB, αC and αD which are associated the some in front of the others. | It is composed to 4 alpha-helix: αA, αB, αC and αD which are associated the some in front of the others. | ||
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The molecule of Erythropoietin have two opposite binding sites with his receptor. The first site include segments of αA, αB and αD and a part of the loop which connects αA and αB. This site include a hydrophobic center which interact with the receptor. | The molecule of Erythropoietin have two opposite binding sites with his receptor. The first site include segments of αA, αB and αD and a part of the loop which connects αA and αB. This site include a hydrophobic center which interact with the receptor. | ||
| - | The Phenylalanine 93 of the receptor is critical important for binding of Erythropoietin to his receptor thanks to hydrogen bonds with residues <scene name='User:Gourinchas_Geoffrey/Sandbox_205/ | + | The Phenylalanine 93 of the receptor is critical important for binding of Erythropoietin to his receptor thanks to hydrogen bonds with residues <scene name='User:Gourinchas_Geoffrey/Sandbox_205/Threonine_44_n2/1'>Threonine 44</scene> and <scene name='User:Gourinchas_Geoffrey/Sandbox_205/Asparagine_147/2'>Asparagine 147</scene> of Erythropoietin. </StructureSection> |
Revision as of 21:56, 27 November 2011
HUMAN ERYTHROPOIETIN
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Erythropoietin is a glycoprotein hormone which is involved in Erythropoiesis, which is the red blood cells production. It allows the differenciation of the erythrocyte precursors in the bone marrow.
Structure
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