1k36: Difference between revisions
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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.]] | ||
[[Category: | [[Category: Egf-like fold]] | ||
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Revision as of 19:14, 2 May 2008
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
