1ern: Difference between revisions

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==Overview==

Erythropoietin receptor (EPOR) is thought to be activated by, ligand-induced homodimerization. However, structures of agonist and, antagonist peptide complexes of EPOR, as well as an EPO-EPOR complex, have, shown that the actual dimer configuration is critical for the biological, response and signal efficiency. The crystal structure of the extracellular, domain of EPOR in its unliganded form at 2.4 angstrom resolution has, revealed a dimer in which the individual membrane-spanning and, intracellular domains would be too far apart to permit phosphorylation by, JAK2. This unliganded EPOR dimer is formed from self-association of the, same key binding site residues that interact with EPO-mimetic peptide and, EPO ligands. This model for a preformed dimer on the cell surface provides, insights into the organization, activation, and plasticity of recognition, of hematopoietic cell surface receptors.

Erythropoietin receptor (EPOR) is thought to be activated by ligand-induced homodimerization. However, structures of agonist and antagonist peptide complexes of EPOR, as well as an EPO-EPOR complex, have shown that the actual dimer configuration is critical for the biological response and signal efficiency. The crystal structure of the extracellular domain of EPOR in its unliganded form at 2.4 angstrom resolution has revealed a dimer in which the individual membrane-spanning and intracellular domains would be too far apart to permit phosphorylation by JAK2. This unliganded EPOR dimer is formed from self-association of the same key binding site residues that interact with EPO-mimetic peptide and EPO ligands. This model for a preformed dimer on the cell surface provides insights into the organization, activation, and plasticity of recognition of hematopoietic cell surface receptors.

==Disease==

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[[Category: Single protein]]

[[Category: Livnah, O.]]

[[Category: Stura, E.A.]]

[[Category: Stura, E A.]]

[[Category: Wilson, I.A.]]

[[Category: Wilson, I A.]]

[[Category: cytokine receptor class 1]]

[[Category: erythropoietin receptor]]

[[Category: signal transduction]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 15~~:44:43 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:31:00 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-Erythropoietin receptor (EPOR) is thought to be activated by, ligand-induced homodimerization. However, structures of agonist and, antagonist peptide complexes of EPOR, as well as an EPO-EPOR complex, have, shown that the actual dimer configuration is critical for the biological, response and signal efficiency. The crystal structure of the extracellular, domain of EPOR in its unliganded form at 2.4 angstrom resolution has, revealed a dimer in which the individual membrane-spanning and, intracellular domains would be too far apart to permit phosphorylation by, JAK2. This unliganded EPOR dimer is formed from self-association of the, same key binding site residues that interact with EPO-mimetic peptide and, EPO ligands. This model for a preformed dimer on the cell surface provides, insights into the organization, activation, and plasticity of recognition, of hematopoietic cell surface receptors.
+Erythropoietin receptor (EPOR) is thought to be activated by ligand-induced homodimerization. However, structures of agonist and antagonist peptide complexes of EPOR, as well as an EPO-EPOR complex, have shown that the actual dimer configuration is critical for the biological response and signal efficiency. The crystal structure of the extracellular domain of EPOR in its unliganded form at 2.4 angstrom resolution has revealed a dimer in which the individual membrane-spanning and intracellular domains would be too far apart to permit phosphorylation by JAK2. This unliganded EPOR dimer is formed from self-association of the same key binding site residues that interact with EPO-mimetic peptide and EPO ligands. This model for a preformed dimer on the cell surface provides insights into the organization, activation, and plasticity of recognition of hematopoietic cell surface receptors.
 ==Disease==
@@ Line 17: / Line 17: @@
 [[Category: Single protein]]
 [[Category: Livnah, O.]]
-[[Category: Stura, E.A.]]
+[[Category: Stura, E A.]]
-[[Category: Wilson, I.A.]]
+[[Category: Wilson, I A.]]
 [[Category: cytokine receptor class 1]]
 [[Category: erythropoietin receptor]]
 [[Category: signal transduction]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:44:43 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:31:00 2008''