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Structures of the human Pals1 PDZ domain with and without ligand suggest gated access of Crb to the PDZ peptide-binding groove.

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Ivanova ME, Fletcher GC, O'Reilly N, Purkiss AG, Thompson BJ, McDonald NQ
OpenAccess logo Acta Crystallogr D Biol Crystallogr 71 555-64 (2015)
Cited: 20 times
EuropePMC logo PMID: 25760605

Abstract

Many components of epithelial polarity protein complexes possess PDZ domains that are required for protein interaction and recruitment to the apical plasma membrane. Apical localization of the Crumbs (Crb) transmembrane protein requires a PDZ-mediated interaction with Pals1 (protein-associated with Lin7, Stardust, MPP5), a member of the p55 family of membrane-associated guanylate kinases (MAGUKs). This study describes the molecular interaction between the Crb carboxy-terminal motif (ERLI), which is required for Drosophila cell polarity, and the Pals1 PDZ domain using crystallography and fluorescence polarization. Only the last four Crb residues contribute to Pals1 PDZ-domain binding affinity, with specificity contributed by conserved charged interactions. Comparison of the Crb-bound Pals1 PDZ structure with an apo Pals1 structure reveals a key Phe side chain that gates access to the PDZ peptide-binding groove. Removal of this side chain enhances the binding affinity by more than fivefold, suggesting that access of Crb to Pals1 may be regulated by intradomain contacts or by protein-protein interaction.

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  1. Synthetic Protein Scaffolds Based on Peptide Motifs and Cognate Adaptor Domains for Improving Metabolic Productivity. Horn AH, Sticht H. Front Bioeng Biotechnol 3 191 (2015)

Articles - 4uu5 mentioned but not cited (9)

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  2. Improved binding of SARS-CoV-2 Envelope protein to tight junction-associated PALS1 could play a key role in COVID-19 pathogenesis. De Maio F, Lo Cascio E, Babini G, Sali M, Della Longa S, Tilocca B, Roncada P, Arcovito A, Sanguinetti M, Scambia G, Urbani A. Microbes Infect 22 592-597 (2020)
  3. Comparing the binding properties of peptides mimicking the Envelope protein of SARS-CoV and SARS-CoV-2 to the PDZ domain of the tight junction-associated PALS1 protein. Toto A, Ma S, Malagrinò F, Visconti L, Pagano L, Stromgaard K, Gianni S. Protein Sci 29 2038-2042 (2020)
  4. Structural basis of coronavirus E protein interactions with human PALS1 PDZ domain. Javorsky A, Humbert PO, Kvansakul M. Commun Biol 4 724 (2021)
  5. Structures of the human Pals1 PDZ domain with and without ligand suggest gated access of Crb to the PDZ peptide-binding groove. Ivanova ME, Fletcher GC, O'Reilly N, Purkiss AG, Thompson BJ, McDonald NQ. Acta Crystallogr D Biol Crystallogr 71 555-564 (2015)
  6. Structural determinants driving the binding process between PDZ domain of wild type human PALS1 protein and SLiM sequences of SARS-CoV E proteins. Lo Cascio E, Toto A, Babini G, De Maio F, Sanguinetti M, Mordente A, Della Longa S, Arcovito A. Comput Struct Biotechnol J 19 1838-1847 (2021)
  7. Interactions of Severe Acute Respiratory Syndrome Coronavirus 2 Protein E With Cell Junctions and Polarity PSD-95/Dlg/ZO-1-Containing Proteins. Zhu Y, Alvarez F, Wolff N, Mechaly A, Brûlé S, Neitthoffer B, Etienne-Manneville S, Haouz A, Boëda B, Caillet-Saguy C. Front Microbiol 13 829094 (2022)
  8. Modeling beta-sheet peptide-protein interactions: Rosetta FlexPepDock in CAPRI rounds 38-45. Khramushin A, Marcu O, Alam N, Shimony O, Padhorny D, Brini E, Dill KA, Vajda S, Kozakov D, Schueler-Furman O. Proteins 88 1037-1049 (2020)
  9. research-article Functional Protein Dynamics in a Crystal. Klyshko E, Sung-Ho Kim J, McGough L, Valeeva V, Lee E, Ranganathan R, Rauscher S. bioRxiv 2023.07.06.548023 (2023)


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  1. Structural Features of Tight-Junction Proteins. Heinemann U, Schuetz A. Int J Mol Sci 20 E6020 (2019)
  2. Not Just Another Scaffolding Protein Family: The Multifaceted MPPs. Chytła A, Gajdzik-Nowak W, Olszewska P, Biernatowska A, Sikorski AF, Czogalla A. Molecules 25 E4954 (2020)

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  1. Crumbs is an essential regulator of cytoskeletal dynamics and cell-cell adhesion during dorsal closure in Drosophila. Flores-Benitez D, Knust E. Elife 4 e07398 (2015)
  2. The cytoskeletal motor proteins Dynein and MyoV direct apical transport of Crumbs. Aguilar-Aragon M, Fletcher G, Thompson BJ. Dev Biol 459 126-137 (2020)
  3. Crumbs organizes the transport machinery by regulating apical levels of PI(4,5)P2 in Drosophila. Lattner J, Leng W, Knust E, Brankatschk M, Flores-Benitez D. Elife 8 e50900 (2019)
  4. Spectroscopic (far or terahertz, mid-infrared and Raman) investigation, thermal analysis and biological activity of piplartine. Srivastava A, Karthick T, Joshi BD, Mishra R, Tandon P, Ayala AP, Ellena J. Spectrochim Acta A Mol Biomol Spectrosc 184 368-381 (2017)
  5. Structure of a Potential Therapeutic Antibody Bound to Interleukin-16 (IL-16): MECHANISTIC INSIGHTS AND NEW THERAPEUTIC OPPORTUNITIES. Hall G, Cullen E, Sawmynaden K, Arnold J, Fox S, Cowan R, Muskett FW, Matthews D, Merritt A, Kettleborough C, Cruikshank W, Taylor D, Bayliss R, Carr MD. J Biol Chem 291 16840-16848 (2016)
  6. The Flexible, Extended Coil of the PDZ-Binding Motif of the Three Deadly Human Coronavirus E Proteins Plays a Role in Pathogenicity. Schoeman D, Cloete R, Fielding BC. Viruses 14 1707 (2022)
  7. Rational design of cyclic peptides to disrupt TGF-Β/SMAD7 signaling in heterotopic ossification. Zhong B, Zhang C, Guo S, Zhang C. J Mol Graph Model 72 25-31 (2017)
  8. Using the inner membrane of Escherichia coli as a scaffold to anchor enzymes for metabolic flux enhancement. Wang Y, Wang Y, Wu Y, Suo Y, Guo H, Yu Y, Yin R, Xi R, Wu J, Hua N, Zhang Y, Zhang S, Jin Z, He L, Ma G. Eng Life Sci 23 e2200034 (2023)


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