1VA8,4UU5


Conserved Protein Domain Family
PDZ_MPP5-like

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cd06798: PDZ_MPP5-like 
PDZ domain of membrane palmitoylated protein 5 (MPP5), Drosophila Stardust, and related domains
PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP5, Drosophila Stardust, and related domains. MPP5 (also known as MAGUK p55 subfamily member 1, protein associated with Lin-7 1 or PALS1) and Drosophila Stardust are membrane-associated guanylate kinase (MAGUK)-like proteins that serve as signaling and scaffolding proteins, linking different proteins critical to the formation and maintenance of tight junctions (TJ) and apical-basal polarity. Apical-basal polarity determinants cluster in complexes; in particular, the Crumbs complex (Crb, MPP5, and PATJ) and the PAR/aPKC-complex (PAR-3, PAR-6, aPKC) determine the apical plasma membrane domain. Within the Crumbs complex, Crb is stabilized in the plasma membrane by MPP5, which in turn recruits PATJ and Lin-7 to the complex. MPP5 also links the Crumbs complex with the PAR/aPKC-complex. The Drosophila homolog of the Crumbs complex is the (CRB)-Stardust (Sdt)-Discs Lost (Dlt) complex. MPP5 also acts as an interaction partner for SARS-CoV envelope protein E, which results in delayed formation of TJs and dysregulation of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP5-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Statistics
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PSSM-Id: 467259
Aligned: 19 rows
Threshold Bit Score: 127.075
Created: 18-Sep-2007
Updated: 27-Apr-2023
Structure
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Program:
Drawing:
Aligned Rows:
 
peptide binding
Conserved site includes 13 residues -Click on image for an interactive view with Cn3D
Feature 1:peptide binding site [polypeptide binding site]
Evidence:
  • Comment:based on canonical PDZ domains with structure
  • Comment:PDZ domains specifically recognize and bind to short C-terminal peptide motifs, but can also recognize internal peptide motifs and certain lipids
  • Structure:4UU5: PDZ domain of human MPP5 binds protein Crumbs homolog 1 (Crb) C-terminal motif (ERLI); contacts at 4A
    View structure with Cn3D
  • Citation:PMID 9546224

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                    #######        #  #                             #   #  ##            
1VA8_A         27 KIVRIEKardiPLGATVRNEmDSVIISRIVKGGAAEKSGLLHEGDEVLEINGIEIRGKDVNEVFDLLSDMhGTLTFVLIP 106  house mouse
XP_035666745  628 KIVRIDKsq-eALGATVRNEgDAVLIARIVKGGAAEKSGLLHEGDEVLEINGKEVRGKSVNEVSDMMGDAvGTITFLLIP 706 
4UU5_A         10 KIVRIEKardiPLGATVRNEmDSVIISRIVKGGAAEKSGLLHEGDEVLEINGIEIRGKDVNEVFDLLSDMhGTLTFVLIP 89   human
AAL40935      832 RIIQIEKst-ePLGATVRNEgEAVVIGRIVRGGAAEKSGLLHEGDEILEVNGQELRGKTVNEVCALLGAMqGTLTFLIVP 910  fruit fly
EEC03542        6 KIVHIDKtn-ePLGATVRNEgESVIIGRIVKGGAAEKSGLLHEGDEVLEVNGIGMRGKSVNEVCDLLATMtGTLTFLIVP 84   black-legged ...
EFX87598       33 KVISLEKsn-ePLGATVRNDgEAVVVGRIVRGGVAERSGLLHEGDEIVEVNGVEVRGKSINDVCDLVASMtGTITFLIVP 111  Daphnia pulex
XP_006825286  576 KVVRIDKta-ePLGATVRNEgDSIVIGRIVRGGAADKSGLLHEGDEILDINGHEMKGKSVNEVCDLMATMtGTLTFLLIP 654  Saccoglossus ...
XP_013085166  565 RIVHLEKtt-eHLGATVKNEgESVIIARIVKGGAAEKSGLLHEGDEILEVNGVDMRGKNINDVSEMLANMsGTIRFMIIP 643  Biomphalaria ...
XP_013392334  456 RVVRLIKna-dPIGATIRNEdESIVIGRIVKGGAAEKSGLLHEGDEILEVNHINMRGKNVNDVSDMLANMtGTLTFLIYP 534  Lingula anatina
XP_012557503  395 KIVRIDKtn-kPLGATVKNEgDAVIISRIIKGGAAEKSELLHEGDEILEINNQSVKGKNIDEVVELLSELeGTITFVLLP 473  Hydra vulgaris

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