1k36

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(New page: 200px<br /> <applet load="1k36" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k36" /> '''NMR Structure of human Epiregulin'''<br /> ...)
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'''NMR Structure of human Epiregulin'''<br />
'''NMR Structure of human Epiregulin'''<br />
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==About this Structure==
==About this Structure==
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1K36 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=1K36 OCA].
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1K36 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=1K36 OCA].
==Reference==
==Reference==
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[[Category: egf-like fold]]
[[Category: egf-like fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:46:52 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:11:05 2008''

Revision as of 14:11, 15 February 2008


1k36

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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

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