1eba: Difference between revisions

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[[Image:1eba.gif|left|200px]]<br />

[[Image:1eba.gif|left|200px]]<br /><applet load="1eba" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1eba" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1eba, resolution 2.7Å" />

'''COMPLEX BETWEEN THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) RECEPTOR [EBP] AND AN INACTIVE PEPTIDE [EMP33] CONTAINS 3,5-DIBROMOTYROSINE IN POSITION 4 (DENOTED DBY)'''<br />

==Overview==

Dimerization of the erythropoietin (EPO) receptor (EPOR), in the presence, of either natural (EPO) or synthetic (EPO-mimetic peptides, EMPs) ligands, is the principal extracellular event that leads to receptor activation., The crystal structure of the extracellular domain of EPOR bound to an, inactive (antagonist) peptide at 2.7 A resolution has unexpectedly, revealed that dimerization still occurs, but the orientation between, receptor molecules is altered relative to active (agonist) peptide, complexes. Comparison of the biological properties of agonist and, antagonist EMPs with EPO suggests that the extracellular domain, orientation is tightly coupled to the cytoplasmic signaling events and, hence, provides valuable new insights into the design of synthetic ligands, for EPOR and other cytokine receptors.

Dimerization of the erythropoietin (EPO) receptor (EPOR), in the presence of either natural (EPO) or synthetic (EPO-mimetic peptides, EMPs) ligands is the principal extracellular event that leads to receptor activation. The crystal structure of the extracellular domain of EPOR bound to an inactive (antagonist) peptide at 2.7 A resolution has unexpectedly revealed that dimerization still occurs, but the orientation between receptor molecules is altered relative to active (agonist) peptide complexes. Comparison of the biological properties of agonist and antagonist EMPs with EPO suggests that the extracellular domain orientation is tightly coupled to the cytoplasmic signaling events and, hence, provides valuable new insights into the design of synthetic ligands for EPOR and other cytokine receptors.

==Disease==

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==About this Structure==

1EBA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1EBA OCA].

1EBA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EBA OCA].

==Reference==

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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: complex (cytokine receptor/peptide)]]

[[Category: cytokine receptor class 1]]

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[[Category: signal transduction]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov~~ 12 16:41:~~54 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:25:59 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1eba.gif|left|200px]]<br />
+[[Image:1eba.gif|left|200px]]<br /><applet load="1eba" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1eba" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1eba, resolution 2.7&Aring;" />
 '''COMPLEX BETWEEN THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) RECEPTOR [EBP] AND AN INACTIVE PEPTIDE [EMP33] CONTAINS 3,5-DIBROMOTYROSINE IN POSITION 4 (DENOTED DBY)'''<br />
 ==Overview==
-Dimerization of the erythropoietin (EPO) receptor (EPOR), in the presence, of either natural (EPO) or synthetic (EPO-mimetic peptides, EMPs) ligands, is the principal extracellular event that leads to receptor activation., The crystal structure of the extracellular domain of EPOR bound to an, inactive (antagonist) peptide at 2.7 A resolution has unexpectedly, revealed that dimerization still occurs, but the orientation between, receptor molecules is altered relative to active (agonist) peptide, complexes. Comparison of the biological properties of agonist and, antagonist EMPs with EPO suggests that the extracellular domain, orientation is tightly coupled to the cytoplasmic signaling events and, hence, provides valuable new insights into the design of synthetic ligands, for EPOR and other cytokine receptors.
+Dimerization of the erythropoietin (EPO) receptor (EPOR), in the presence of either natural (EPO) or synthetic (EPO-mimetic peptides, EMPs) ligands is the principal extracellular event that leads to receptor activation. The crystal structure of the extracellular domain of EPOR bound to an inactive (antagonist) peptide at 2.7 A resolution has unexpectedly revealed that dimerization still occurs, but the orientation between receptor molecules is altered relative to active (agonist) peptide complexes. Comparison of the biological properties of agonist and antagonist EMPs with EPO suggests that the extracellular domain orientation is tightly coupled to the cytoplasmic signaling events and, hence, provides valuable new insights into the design of synthetic ligands for EPOR and other cytokine receptors.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-EBA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EBA OCA].
+EBA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EBA OCA].
 ==Reference==
@@ Line 18: / 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: complex (cytokine receptor/peptide)]]
 [[Category: cytokine receptor class 1]]
@@ Line 27: / Line 26: @@
 [[Category: signal transduction]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:41:54 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:25:59 2008''