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PDBsum entry 1k37
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Hormone/growth factor
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PDB id
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1k37
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Solution structure of epiregulin and the effect of its c-Terminal domain for receptor binding affinity.
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Authors
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K.Sato,
T.Nakamura,
M.Mizuguchi,
K.Miura,
M.Tada,
T.Aizawa,
T.Gomi,
K.Miyamoto,
K.Kawano.
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Ref.
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FEBS Lett, 2003,
553,
232-238.
[DOI no: ]
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PubMed id
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Abstract
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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.
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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].
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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.
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The above figures are
reprinted
by permission from the Federation of European Biochemical Societies:
FEBS Lett
(2003,
553,
232-238)
copyright 2003.
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