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PDBsum entry 1ivo
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Transferase/signaling protein
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PDB id
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1ivo
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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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Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains.
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Authors
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H.Ogiso,
R.Ishitani,
O.Nureki,
S.Fukai,
M.Yamanaka,
J.H.Kim,
K.Saito,
A.Sakamoto,
M.Inoue,
M.Shirouzu,
S.Yokoyama.
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Ref.
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Cell, 2002,
110,
775-787.
[DOI no: ]
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PubMed id
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Abstract
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Epidermal growth factor (EGF) regulates cell proliferation and differentiation
by binding to the EGF receptor (EGFR) extracellular region, comprising domains
I-IV, with the resultant dimerization of the receptor tyrosine kinase. In this
study, the crystal structure of a 2:2 complex of human EGF and the EGFR
extracellular region has been determined at 3.3 A resolution. EGFR domains I-III
are arranged in a C shape, and EGF is docked between domains I and III. The 1:1
EGF*EGFR complex dimerizes through a direct receptor*receptor interaction, in
which a protruding beta-hairpin arm of each domain II holds the body of the
other. The unique "receptor-mediated dimerization" was verified by
EGFR mutagenesis.
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Figure 3.
Figure 3. Interactions between EGF and EGFREGF and the EGFR
domains are colored in the same manner as in Figure 1, except
for (B).(A) Mapping the interaction sites onto ribbon
representations of EGFR and EGF. Three binding sites in the
interface are outlined.(B) EGF structure. The A, B, and C loops
are colored blue, green, and red, respectively. The other
regions are pale green.(C) Stereo view of the interface at site
1. Only the side chains of interacting residues are shown.
Dotted lines represent hydrogen bonds.(D) Stereo view of the
interface at site 2.(E) Stereo view of the interface at site 3.
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Figure 4.
Figure 4. Interactions between Each Receptor in the Dimer
Interface(A) The binding region in the interface is outlined.
Only the side chains of interacting residues are shown. EGF and
the EGFR domains are colored in the same manner as in Figure
1.(B) Stereo view of an annealed omit map. Residues 240–260
and the residues within 3.5 Å from them of one EGRF
molecule (orange) were omitted.(C) Stereo view of the interface
from the view shown by the arrow in (A); the view is directed
from the front side of domain I toward Y251 of the other
receptor. Dotted lines represent hydrogen bonds.(D) Stereo view
of the interface from the view shown by the arrow in (A); the
view is directed from the back side of domain I toward Y251 of
the other receptor.
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The above figures are
reprinted
by permission from Cell Press:
Cell
(2002,
110,
775-787)
copyright 2002.
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