1. The Structure of the PDZ3-SH3-GuK Tandem of ZO-1 Protein Suggests a Supramodular Organization of the Membrane-associated Guanylate Kinase (MAGUK) Family Scaffold Protein Core
- Author
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Haoyue Yu, Jiang Yu, Mingjie Zhang, Jia Chen, and Lifeng Pan
- Subjects
Scaffold protein ,Guanylate kinase ,Protein domain ,PDZ domain ,Membrane Proteins ,Cell Biology ,Membrane-associated guanylate kinase ,Biology ,Crystallography, X-Ray ,Phosphoproteins ,Biochemistry ,Cell biology ,src Homology Domains ,Structure-Activity Relationship ,Protein structure ,Membrane protein ,Guanylate Cyclase ,Protein Structure and Folding ,Zonula Occludens-1 Protein ,Humans ,Molecular Biology ,Proto-oncogene tyrosine-protein kinase Src - Abstract
Membrane-associated guanylate kinases (MAGUKs) are a large family of scaffold proteins that play essential roles in tethering membrane receptors, adhesion molecules, and macromolecular signaling complexes for tissue developments, cell-cell communications, and intracellular signal transductions. The defining feature of the MAGUK family scaffolds is that each member contains a conserved core consisting of a PSD-95/Dlg/ZO-1 (PDZ) domain, an Src homology 3 (SH3) domain, and a catalytically inactive guanylate kinase (GuK) domain arranged in tandem, although the structural features and functional implications of the PDZ-SH3-GuK tandem arrangement are unclear. The structure of the ZO-1 PDZ3-SH3-GuK tandem solved in this study reveals that the PDZ domain directly interacts with the SH3-GuK module, forming a structural supramodule with distinct target binding properties with respect to the isolated domains. Structure-based sequence analysis suggests that the PDZ-SH3-GuK tandems of other members of the MAGUK family also form supramodules.
- Published
- 2011
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