User:Gourinchas Geoffrey/Sandbox 205
From Proteopedia
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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. | 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. | ||
| - | In the second interaction site the Methionine 150 | + | In the second interaction site, the Methionine 150 allows van der waals interactions with Arginine 10, the Valine 11 and the Arginine 14 of Erythropoietin. |
| - | The hydrophobic interaction include 11 hydrogen bonds between αA and αC of Erythropoietin and his receptor. </StructureSection> | + | The hydrophobic interaction include 11 hydrogen bonds between αA and αC of Erythropoietin and his receptor. |
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| + | == '''Optimal angle for Erythropoietin binding to his receptor.''' == [[Image:orientation.jpg]] | ||
| + | Syed and al. in 1998 have showed that Erythropoietin optimal binds at his receptor if only there is an angle of 120° between the two sites of the receptor. | ||
| + | The intracellular surface create by ths angle of 120° allows the optimal induction of Erythropoietin by the intracellulaire way of Kinase. </StructureSection> | ||
Revision as of 12:37, 28 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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