1k36

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[[Image:1k36.jpg|left|200px]]
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{{Structure
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|RELATEDENTRY=[[1k37|1K37]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k36 OCA], [http://www.ebi.ac.uk/pdbsum/1k36 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k36 RCSB]</span>
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'''NMR Structure of human Epiregulin'''
'''NMR Structure of human Epiregulin'''
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[[Category: Sato, K.]]
[[Category: Sato, K.]]
[[Category: Tada, M.]]
[[Category: Tada, M.]]
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[[Category: egf-like fold]]
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[[Category: Egf-like fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:14:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:42:42 2008''
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Revision as of 19:14, 2 May 2008

Image:1k36.jpg

Template:STRUCTURE 1k36

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 Fri May 2 22:14:44 2008

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