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PDBsum entry 4wyu
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Structural protein/peptide
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PDB id
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4wyu
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References listed in PDB file
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Key reference
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Title
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Interdomain interface-Mediated target recognition by the scribble pdz34 supramodule.
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Authors
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J.Ren,
L.Feng,
Y.Bai,
H.Pei,
Z.Yuan,
W.Feng.
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Ref.
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Biochem J, 2015,
468,
133-144.
[DOI no: ]
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PubMed id
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Abstract
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Tandem-arranged PDZ [PSD-95 (postsynaptic density-95), Dlg (discs large
homologue) and ZO-1 (zonula occludens-1)] domains often form structural and
functional supramodules with distinct target-binding properties. In the present
study, we found that the two PDZ domains within the PDZ34 tandem of Scribble, a
cell polarity regulator, tightly pack in a 'front-to-back' mode to form a
compact supramodule. Although PDZ4 contains a distorted αB/βB pocket, the
attachment of PDZ4 to PDZ3 generates an unexpected interdomain pocket that is
adjacent to and integrates with the canonical αB/βB pocket of PDZ3 to form an
expanded target-binding groove. The structure of the PDZ34-target peptide
complex further demonstrated that the peptide binds to this expanded
target-binding groove with its upstream residues anchoring into the interdomain
pocket directly. Mutations of the interdomain pocket and disruptions of the
PDZ34 supramodule both interfere with its target-binding capacity. Therefore,
the interdomain interface between the PDZ34 supramodule is intrinsically
required for its target recognition and determines its target-binding
specificity. This interdomain interface-mediated specific recognition may
represent a novel mode of target recognition and would broaden the
target-binding versatility for PDZ supramodules. The supramodular nature and
target recognition mode of the PDZ34 tandem found in the present study would
also help to identify the new binding partners of Scribble and thus may direct
further research on the PDZ domain-mediated assembly of Scribble polarity
complexes.
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