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PDBsum entry 1w9q
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Cell adhesion
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PDB id
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1w9q
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References listed in PDB file
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Key reference
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Title
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The binding of the pdz tandem of syntenin to target proteins.
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Authors
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J.Grembecka,
T.Cierpicki,
Y.Devedjiev,
U.Derewenda,
B.S.Kang,
J.H.Bushweller,
Z.S.Derewenda.
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Ref.
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Biochemistry, 2006,
45,
3674-3683.
[DOI no: ]
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PubMed id
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Abstract
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PDZ domains are among the most abundant protein modules in the known genomes.
Their main function is to provide scaffolds for membrane-associated protein
complexes by binding to the cytosolic, C-terminal fragments of receptors,
channels, and other integral membrane proteins. Here, using both heteronuclear
NMR and single crystal X-ray diffraction, we show how peptides with different
sequences, including those corresponding to the C-termini of syndecan, neurexin,
and ephrin B, can simultaneously bind to both PDZ domains of the scaffolding
protein syntenin. The PDZ2 domain binds these peptides in the canonical fashion,
and an induced fit mechanism allows for the accommodation of a range of side
chains in the P(0) and P(-)(2) positions. However, binding to the PDZ1 domain
requires that the target peptide assume a noncanonical conformation. These data
help explain how syntenin, and perhaps other PDZ-containing proteins, may
preferentially bind to dimeric and clustered targets, and provide a mechanistic
explanation for the previously reported cooperative ligand binding by syntenin's
two PDZ domains.
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