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1k36
From Proteopedia
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| - | [[Image:1k36.jpg|left|200px]] | + | [[Image:1k36.jpg|left|200px]] |
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| - | '''NMR Structure of human Epiregulin''' | + | {{Structure |
| + | |PDB= 1k36 |SIZE=350|CAPTION= <scene name='initialview01'>1k36</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''NMR Structure of human Epiregulin''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1K36 is a [ | + | 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]. |
==Reference== | ==Reference== | ||
| - | Solution structure of epiregulin and the effect of its C-terminal domain for receptor binding affinity., Sato K, Nakamura T, Mizuguchi M, Miura K, Tada M, Aizawa T, Gomi T, Miyamoto K, Kawano K, FEBS Lett. 2003 Oct 23;553(3):232-8. PMID:[http:// | + | Solution structure of epiregulin and the effect of its C-terminal domain for receptor binding affinity., Sato K, Nakamura T, Mizuguchi M, Miura K, Tada M, Aizawa T, Gomi T, Miyamoto K, Kawano K, FEBS Lett. 2003 Oct 23;553(3):232-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14572630 14572630] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: egf-like fold]] | [[Category: egf-like fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:11:56 2008'' |
Revision as of 10:11, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
About this Structure
1K36 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of epiregulin and the effect of its C-terminal domain for receptor binding affinity., Sato K, Nakamura T, Mizuguchi M, Miura K, Tada M, Aizawa T, Gomi T, Miyamoto K, Kawano K, FEBS Lett. 2003 Oct 23;553(3):232-8. PMID:14572630
Page seeded by OCA on Thu Mar 20 12:11:56 2008
