1k36
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1k37|1K37]] | ||
| + | |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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[[Category: egf-like fold]] | [[Category: egf-like fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:42:42 2008'' |
Revision as of 18:42, 30 March 2008
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| Related: | 1K37
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
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