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PDBsum entry 1obx
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Cell adhesion
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PDB id
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1obx
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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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Molecular roots of degenerate specificity in syntenin'S pdz2 domain: reassessment of the pdz recognition paradigm.
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Authors
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B.S.Kang,
D.R.Cooper,
Y.Devedjiev,
U.Derewenda,
Z.S.Derewenda.
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Ref.
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Structure, 2003,
11,
845-853.
[DOI no: ]
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PubMed id
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Abstract
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Crystal structures of the PDZ2 domain of the scaffolding protein syntenin, both
unbound and in complexes with peptides derived from C termini of IL5 receptor
(alpha chain) and syndecan, reveal the molecular roots of syntenin's degenerate
specificity. Three distinct binding sites (S(0), S(-1), and S(-2)), with
affinities for hydrophobic side chains, function in a combinatorial way: S(-1)
and S(-2) act together to bind syndecan, while S(0) and S(-1) are involved in
the binding of IL5Ralpha. Neither mode of interaction is consistent with the
prior classification scheme, which defined the IL5Ralpha interaction as class I
(-S/T-X-phi) and the syndecan interaction as class II (-phi-X-phi). These
results, in conjunction with other emerging structural data on PDZ domains, call
for a revision of their classification and of the existing model of their
mechanism.
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Figure 3.
Figure 3. Schematics of PDZ Interactions(A) Canonical PDZ
binding of C-terminal sequence depends on the residues P[0] and
P[ -2] binding pockets S[0] and S[ -2].(B) All three C-terminal
residues are involved in the interaction to PDZ binding
groove.(C) The C-terminal binding depends on the binding at S[
-1] and S[ -2] of PDZ as seen in PDZ2-syndecan-4 peptide
complex.(D) The C-terminal binding depends on the binding at
S[0] and S[ -1] as seen in syntenin PDZ2-interleukin 5 receptor
a subunit peptide complex.(E) Syntrophin PDZ interaction by the
residues from b-finger conformation of nNOS.(F) Interaction of
internal residue at pocket S[ -2] while C-terminal residues
binds at S[0] as seen in syntenin PDZ2-PDZ2 interaction.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2003,
11,
845-853)
copyright 2003.
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