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PDBsum entry 3tsv
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Cell adhesion
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PDB id
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3tsv
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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 src homology 3 domain is required for junctional adhesion molecule binding to the third pdz domain of the scaffolding protein zo-1.
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Authors
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J.Nomme,
A.S.Fanning,
M.Caffrey,
M.F.Lye,
J.M.Anderson,
A.Lavie.
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Ref.
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J Biol Chem, 2011,
286,
43352-43360.
[DOI no: ]
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PubMed id
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Abstract
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Tight junctions are cell-cell contacts that regulate the paracellular flux of
solutes and prevent pathogen entry across cell layers. The assembly and
permeability of this barrier are dependent on the zonula occludens (ZO)
membrane-associated guanylate kinase (MAGUK) proteins ZO-1, -2, and -3. MAGUK
proteins are characterized by a core motif of protein-binding domains that
include a PDZ domain, a Src homology 3 (SH3) domain, and a region of homology to
guanylate kinase (GUK); the structure of this core motif has never been
determined for any MAGUK. To better understand how ZO proteins organize the
assembly of protein complexes we have crystallized the entire PDZ3-SH3-GUK core
motif of ZO-1. We have also crystallized this core motif in complex with the
cytoplasmic tail of the ZO-1 PDZ3 ligand, junctional adhesion molecule A (JAM-A)
to determine how the activity of different domains is coordinated. Our study
shows a new feature for PDZ class II ligand binding that implicates the two
highly conserved Phe(-2) and Ser(-3) residues of JAM. Our x-ray structures and
NMR experiments also show for the first time a role for adjacent domains in the
binding of ligands to PDZ domains in the MAGUK proteins family.
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