PDBsum entry 1k37

Hormone/growth factor

PDB id: 1k37

Contents

Protein chain

46 a.a. *

* Residue conservation analysis

PDB id:

1k37

Name:

Hormone/growth factor

Title:

Nmr structure of human epiregulin

Structure:

Epiregulin. Chain: a. Fragment: residues 1-46. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

1 models

Authors:

K.Sato,K.Miura,M.Tada,T.Aizawa,K.Miyamoto,K.Kawano

Key ref:

K.Sato et al. (2003). Solution structure of epiregulin and the effect of its C-terminal domain for receptor binding affinity. FEBS Lett, 553, 232-238. PubMed id: 14572630 DOI: 10.1016/S0014-5793(03)01005-6

Date:

02-Oct-01 Release date: 30-Sep-03

Protein chain

O14944  (EREG_HUMAN) -  Proepiregulin from Homo sapiens

Seq: 169 a.a.

Struc: 46 a.a.

DOI no: 10.1016/S0014-5793(03)01005-6

FEBS Lett 553:232-238 (2003)

PubMed id: 14572630

Solution structure of epiregulin and the effect of its C-terminal domain for receptor binding affinity.

K.Sato, T.Nakamura, M.Mizuguchi, K.Miura, M.Tada, T.Aizawa, T.Gomi, K.Miyamoto, K.Kawano.

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.

Selected figure(s)

Figure 2.
Fig. 2. Tertiary structure of EPR. A: The ensemble of 40 NMR structures of EPR superimposed and fitted for the backbone atoms of residues 4–44. B: The ribbon drawing of the minimized average structure of EPR. Sequence numbers of some residues are indicated. These diagrams were generated using the program MOLMOL [30].

Figure 4.
Fig. 4. A: Comparison of the structure in the C-terminal domain between EPR and EGF. Hydrogen bonds between Ser^38 and Thr^44 in EGF are shown by continuous lines with the hydrogen bond lengths. The lengths between backbone NH and O atoms in EPR are shown by dotted lines. Backbone NH and O atoms are represented by blue and red, respectively. B: Comparison of the hydrogen bond lengths (Å) in the C-terminal domain among EGF-family ligands. The lengths between backbone NH and O atoms in EPR are shown for comparison.

The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (2003, 553, 232-238) copyright 2003.

Figures were selected by an automated process.