1k36: Difference between revisions

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[[Image:1k36.~~jpg~~|left|200px]]

[[Image:1k36.png|left|200px]]

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~~'''~~NMR Structure of human Epiregulin~~'''~~

===NMR Structure of human Epiregulin===

~~==Overview==~~

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~~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.

The line below this paragraph, {{ABSTRACT_PUBMED_14572630}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 14572630 is the PubMed ID number.

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==About this Structure==

1K36 is a [[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=1K36 OCA].

1K36 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K36 OCA].

==Reference==

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[[Category: Tada, M.]]

[[Category: Egf-like fold]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 22~~:14:44 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:52:17 2008''

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-[[Image:1k36.jpg|left|200px]]
+{{Seed}}
+[[Image:1k36.png|left|200px]]
 <!--
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 {{STRUCTURE_1k36|  PDB=1k36  |  SCENE=  }}
-'''NMR Structure of human Epiregulin'''
+===NMR Structure of human Epiregulin===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_14572630}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14572630 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14572630}}
 ==About this Structure==
-K36 is a [[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=1K36 OCA].
+K36 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K36 OCA].
 ==Reference==
@@ Line 29: / Line 33: @@
 [[Category: Tada, M.]]
 [[Category: Egf-like fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 22:14:44 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:52:17 2008''