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==Overview==

Epiregulin (EPR), a novel member of epidermal growth factor (EGF) family, is a ligand for ErbB-1 and ErbB-4 receptors. The binding affinity of EPR, for the receptors is lower than those of other EGF-family ligands. The, solution structure of EPR was determined using two-dimensional nuclear, magnetic resonance spectroscopy. The secondary structure in the C-terminal, domain of EPR is different from other EGF-family ligands because of the, lack of hydrogen bonds. The structural difference in the C-terminal domain, may provide an explanation for the reduced binding affinity of EPR to the, ErbB receptors.

Epiregulin (EPR), a novel member of epidermal growth factor (EGF) family, is a ligand for ErbB-1 and ErbB-4 receptors. The binding affinity of EPR for the receptors is lower than those of other EGF-family ligands. The solution structure of EPR was determined using two-dimensional nuclear magnetic resonance spectroscopy. The secondary structure in the C-terminal domain of EPR is different from other EGF-family ligands because of the lack of hydrogen bonds. The structural difference in the C-terminal domain may provide an explanation for the reduced binding affinity of EPR to the ErbB receptors.

==About this Structure==

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[[Category: egf-like fold]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 16~~:11:05 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:29:38 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-Epiregulin (EPR), a novel member of epidermal growth factor (EGF) family, is a ligand for ErbB-1 and ErbB-4 receptors. The binding affinity of EPR, for the receptors is lower than those of other EGF-family ligands. The, solution structure of EPR was determined using two-dimensional nuclear, magnetic resonance spectroscopy. The secondary structure in the C-terminal, domain of EPR is different from other EGF-family ligands because of the, lack of hydrogen bonds. The structural difference in the C-terminal domain, may provide an explanation for the reduced binding affinity of EPR to the, ErbB receptors.
+Epiregulin (EPR), a novel member of epidermal growth factor (EGF) family, is a ligand for ErbB-1 and ErbB-4 receptors. The binding affinity of EPR for the receptors is lower than those of other EGF-family ligands. The solution structure of EPR was determined using two-dimensional nuclear magnetic resonance spectroscopy. The secondary structure in the C-terminal domain of EPR is different from other EGF-family ligands because of the lack of hydrogen bonds. The structural difference in the C-terminal domain may provide an explanation for the reduced binding affinity of EPR to the ErbB receptors.
 ==About this Structure==
@@ Line 21: / Line 21: @@
 [[Category: egf-like fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:11:05 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:29:38 2008''