Novel Mode of Ligand Recognition by the Erbin PDZ Domain*
@article{Birrane2003NovelMO, title={Novel Mode of Ligand Recognition by the Erbin PDZ Domain*}, author={Gabriel Birrane and Ju Young Chung and John A. A. Ladias}, journal={The Journal of Biological Chemistry}, year={2003}, volume={278}, pages={1399 - 1402} }
Erbin contains a class I PDZ domain that binds to the C-terminal region of the receptor tyrosine kinase ErbB2, a class II ligand. The crystal structure of the human Erbin PDZ bound to the peptide EYLGLDVPV corresponding to the C-terminal residues 1247–1255 of human ErbB2 has been determined at 1.25-Å resolution. The Erbin PDZ deviates from the canonical PDZ fold in that it contains a single α-helix. The isopropyl group of valine at position −2 of the ErbB2 peptide interacts with the Erbin…
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References
SHOWING 1-10 OF 31 REFERENCES
The PDZ1 Domain of SAP90
- Biology, ChemistryThe Journal of Biological Chemistry
- 2002
Describing the association of PDZ1 to the C-terminal peptides of the GluR6 subunit of the kainate receptor, voltage-gated K+ channel Kv1.4, and microtubule-associate protein CRIPT shows specific differences are present, consistent with the variation in binding affinities.
The Erbin PDZ Domain Binds with High Affinity and Specificity to the Carboxyl Termini of δ-Catenin and ARVCF*
- Biology, ChemistryThe Journal of Biological Chemistry
- 2002
Results suggest that δ-catenin and ARVCF may function to mediate the association of Erbin with the junctional cadherin-Catenin complex and demonstrate that C-terminal phage-display technology can be used to predict physiologically relevant ligands for PDZ domains.
ERBIN: a basolateral PDZ protein that interacts with the mammalian ERBB2/HER2 receptor
- BiologyNature Cell Biology
- 2000
It is suggested that ERBIN acts in the localization and signalling of ERBB2/HER2 in epithelia and belongs to a new PDZ protein family.
Solution structure of the PDZ2 domain from cytosolic human phosphatase hPTP1E complexed with a peptide reveals contribution of the beta2-beta3 loop to PDZ domain-ligand interactions.
- Chemistry, BiologyJournal of molecular biology
- 2002
PDZ domains and the organization of supramolecular complexes.
- BiologyAnnual review of neuroscience
- 2001
PDZ domains are modular protein interaction domains that bind in a sequence-specific fashion to short C-terminal peptides or internal peptides that fold in a beta-finger. The diversity of PDZ binding…
Structural Basis of the Na+/H+ Exchanger Regulatory Factor PDZ1 Interaction with the Carboxyl-terminal Region of the Cystic Fibrosis Transmembrane Conductance Regulator*
- Biology, ChemistryThe Journal of Biological Chemistry
- 2001
The crystal structure of human NHERF PDZ1 bound to the carboxyl-terminal peptide QDTRL has been determined and reveals the specificity and affinity determinants of thePDZ1-CFTR interaction and provides insights into car boxyl- terminal leucine recognition by class I PDZ domains.
Ligand Binding of the Second PDZ Domain Regulates Clustering of PSD-95 with the Kv1.4 Potassium Channel*
- Biology, ChemistryThe Journal of Biological Chemistry
- 2002
This study suggests that the correct placement of the multiple domains in the full-length PSD-95 protein is necessary for the optimal protein activity, and shows that PDZ2, which is endowed with the highest affinity for Kv1.4, is required for efficient ligand binding.
Structural Determinants of the Na+/H+Exchanger Regulatory Factor Interaction with the β2Adrenergic and Platelet-derived Growth Factor Receptors*
- Chemistry, BiologyThe Journal of Biological Chemistry
- 2002
Structural insights are provided into the mechanisms by which different side chains at the position −1 of peptide ligands interact with PDZ domains and contribute to the affinity of the PDZ-ligand interaction.
A single autophosphorylation site confers oncogenicity to the Neu/ErbB‐2 receptor and enables coupling to the MAP kinase pathway.
- Biology, ChemistryThe EMBO journal
- 1994
The results indicate that the multiplicity of autophosphorylation sites on a receptor tyrosine kinase is not essential for transformability, and implicate the MAP kinase pathway in transduction of the oncogenic signal of Neu/ErbB‐2.
Multiple ErbB-2/Neu Phosphorylation Sites Mediate Transformation through Distinct Effector Proteins*
- BiologyThe Journal of Biological Chemistry
- 2001
The results showed that Grb2 recruitment to site 1144 is absolutely required for transforming signal from this autophosphorylation site, whereas association of Shc-mediated transformation is dependent on conservation of the NPXY motif spanning Tyr1227.