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Contents |
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* Residue conservation analysis
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DOI no:
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Science
287:1279-1283
(2000)
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PubMed id:
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Convergent solutions to binding at a protein-protein interface.
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W.L.DeLano,
M.H.Ultsch,
A.M.de Vos,
J.A.Wells.
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ABSTRACT
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The hinge region on the Fc fragment of human immunoglobulin G interacts with at
least four different natural protein scaffolds that bind at a common site
between the C(H2) and C(H3) domains. This "consensus" site was also
dominant for binding of random peptides selected in vitro for high affinity
(dissociation constant, about 25 nanomolar) by bacteriophage display. Thus, this
site appears to be preferred owing to its intrinsic physiochemical properties,
and not for biological function alone. A 2.7 angstrom crystal structure of a
selected 13-amino acid peptide in complex with Fc demonstrated that the peptide
adopts a compact structure radically different from that of the other Fc binding
proteins. Nevertheless, the specific Fc binding interactions of the peptide
strongly mimic those of the other proteins. Juxtaposition of the available
Fc-complex crystal structures showed that the convergent binding surface is
highly accessible, adaptive, and hydrophobic and contains relatively few sites
for polar interactions. These are all properties that may promote cross-reactive
binding, which is common to protein-protein interactions and especially
hormone-receptor complexes.
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Selected figure(s)
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Figure 2.
Fig. 2. Crystal structure of Fc-III (DCAWHLGELVWCT-NH[2]), in
complex with IgG-Fc. (A) Ribbon diagrams of two Fc-III peptides
in complex with the Fc dimer; (B) close-up view of the peptide
interacting with the surface of IgG-Fc. This structure has been
deposited in the PDB under accession number 1DN2.
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Figure 3.
Fig. 3. Molecular surface representation of the consensus
binding site on IgG-Fc [coordinates from Deisenhofer (3)]. (A)
Fc with superimposed binding interfaces of Protein A, Protein G,
and rheumatoid factor. (The 4.5 Å crystal structure of the
Fc-receptor/Fc complex was excluded because of its low
resolution.) Atoms are colored blue, yellow, or red depending on
whether they are involved in one, two, or three of the
interfaces, respectively (17). (B) As in (A) with the interface
of the Fc binding peptide (Fc-III) superimposed in green. Fc-III
interacts with many of the atoms that are found in the
interfaces of the other three Fc binding proteins.
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The above figures are
reprinted
by permission from the AAAs:
Science
(2000,
287,
1279-1283)
copyright 2000.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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PDB codes:
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PDB codes:
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PDB code:
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PDB codes:
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PDB code:
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M.J.Boulanger,
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Mol Cell,
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PDB code:
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M.R.Arkin,
M.Randal,
W.L.DeLano,
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Proc Natl Acad Sci U S A,
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PDB codes:
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Biophys J,
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Chembiochem,
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Mol Cell,
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PDB code:
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One from column A and two from column B: the benefits of phage display in molecular-recognition studies.
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Proteins,
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PDB code:
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Biochemistry,
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PDB codes:
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P.Zhou,
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PDB code:
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Mol Microbiol,
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Crystal structure at 2.8 A of an FcRn/heterodimeric Fc complex: mechanism of pH-dependent binding.
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Mol Cell,
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PDB codes:
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A.G.Cochran
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Crystal structure of the catalytic domain of human bile salt activated lipase.
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Protein Sci,
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PDB code:
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EMBO J,
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PDB codes:
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|
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|
|
The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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 |
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