1K37

NMR Structure of human Epiregulin

Summary for 1K37

• Entry DOI: 10.2210/pdb1k37/pdb
• Related: 1K36
• NMR Information: BMRB: 5173
• Descriptor: Epiregulin (1 entity in total)
• Functional Keywords: egf-like fold, hormone-growth factor complex, hormone/growth factor
• Biological source: Homo sapiens (human)
• Cellular location: Epiregulin: Secreted, extracellular space. Proepiregulin: Cell membrane; Single-pass type I membrane protein: O14944
• Total number of polymer chains: 1
• Total formula weight: 5280.07

Authors

Sato, K.,Miura, K.,Tada, M.,Aizawa, T.,Miyamoto, K.,Kawano, K. (deposition date: 2001-10-02, release date: 2003-09-30, Last modification date: 2024-10-23)

Primary citation

Sato, K.,Nakamura, T.,Mizuguchi, M.,Miura, K.,Tada, M.,Aizawa, T.,Gomi, T.,Miyamoto, K.,Kawano, K.
Solution structure of epiregulin and the effect of its C-terminal domain for receptor binding affinity
Febs Lett., 553:232-238, 2003

PubMed Abstract: 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.

PubMed: 14572630
DOI: 10.1016/S0014-5793(03)01005-6

Experimental method

SOLUTION NMR