4OEP,2RRM,2CSJ,4YYX


Conserved Protein Domain Family
PDZ1_ZO1-like

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cd06727: PDZ1_ZO1-like 
PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains
PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of ZO-1, -2, -3 and related domains. Zonula occludens proteins (ZO-1, ZO-2, ZO-3) are multi-PDZ domain proteins involved in the maintenance and biogenesis of multi-protein networks at the cytoplasmic surface of intercellular contacts in epithelial and endothelial cells. They have three N-terminal PDZ domains, PDZ1-3, followed by a Src homology-3 (SH3) domain and a guanylate kinase (GuK)-like domain. Among protein-protein interactions for all ZO proteins is the binding of the first PDZ domain (PDZ1) to the C-termini of claudins, and the homo- and hetero-dimerization of ZO-proteins via their second PDZ domain (PDZ2), which takes place by symmetrical domain swapping of the first two beta-strands of PDZ2. At the cell level, ZO-1 and ZO-2 are involved in polarity maintenance, gene transcription, cell proliferation, and tumor cell metastasis. 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 ZO family PDZ1 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: 467209
Aligned: 31 rows
Threshold Bit Score: 118.916
Created: 15-Jun-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

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                     #######                 #  #                           #   #  ##    
4OEP_A          9 HTVTLHRAPg-fGFGIAISGGRDNphfqsgetSIVISDVLkGGPAEGQLQENDRVAMVNGVSMDNVEHAFAVQQLRKSgK 87   human
EFX71884       71 HHVTMNRVPg-yGFGIAVSGGRDNphfangdpSIAISDVIkGGPAEGKLLINDRVMSVNGVSLENVDYGTAVSVLRDSgA 149  Daphnia pulex
XP_782687      38 DTVSIRRAQg-lGFGIAVSGGQDNphfssgetSIVVSDVApNGPAEGMLKKNDRILSVNGASMENAYHSDAIGALRHSgE 116  purple sea ur...
XP_002129483    9 HTYVIEKAPg-vGFGIAISGGKDNpgvqsgdtSIILSDVVkQGPAYDKLKINDIVLRVNGRPMYNVAHHQAVKELKNAgH 87   vase tunicate
AAK28322       19 TLVTLEKKSakqGFGIAISGGLDNphfktgdtSIIVSDIVqGSPADGKLKVGDILISVNERNVDGRSHHDAVEALKAAgM 98   Hydra vulgaris
XP_006813237   53 YTVVLDRKPa-fGFGIAVSGGIDNphftsgetSIVISDVLsGGPAEAKLKVNDRVIMVNNRSMENVEHCDAVSALKNSgD 131  Saccoglossus ...
XP_035670915  210 LSFTINRAPg-yGFGIAVSGGRDNphftsgetSIVISDVLpGGPAEGLLKVNDRVVSVNRASLDHVDHSQAVNILKDSrD 288  Branchiostoma...
ELU09381      218 HNVTLSRLPs-fGFGIAVSGGRDNphfsngdtSIAISDVLkAGPAEGKLLINDRILSVNGISLENVDHATAISVLKDSgN 296  Capitella teleta
NP_001097712  305 HTVAVTRVPg-yGFGIAVSGGRDNphfangdpSIAVSDVLkGGPAEDRLQVNDRIISVNGVSLENVEYATAVQVLRDSgN 383  fruit fly
NP_001252376   44 LSVSLHRAAn-lGFGIAISGGRDNphftsgdpVVVISDVVpNGPAWGLLQVNDRILSANQVSFENIEYSSAVDIIKNKdH 122  Caenorhabditi...
Feature 1                 
4OEP_A         88 NAKITIRR 95   human
EFX71884      150 AVNLVVKR 157  Daphnia pulex
XP_782687     117 VVTITYKR 124  purple sea urchin
XP_002129483   88 RVELTIKR 95   vase tunicate
AAK28322       99 EARMEIKR 106  Hydra vulgaris
XP_006813237  132 TATLVVKR 139  Saccoglossus kowalevskii
XP_035670915  289 SAVIVVKR 296  Branchiostoma floridae
ELU09381      297 SVNLVVRR 304  Capitella teleta
NP_001097712  384 TVQLVVKR 391  fruit fly
NP_001252376  123 IDMIVKRR 130  Caenorhabditis elegans

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