Journal of Biomolecular NMR

, Volume 32, Issue 3, pp 209–218 | Cite as

Solution Structure of the Second PDZ Domain of the Neuronal Adaptor X11α and its Interaction with the C-terminal Peptide of the Human Copper Chaperone for Superoxide Dismutase

  • Aude E. Duquesne
  • Martina de Ruijter
  • Jaap Brouwer
  • Jan W. Drijfhout
  • Sander B. Nabuurs
  • Chris A. E. M. Spronk
  • Geerten W. Vuister
  • Marcellus Ubbink
  • Gerard W. Canters
Article

Abstract

Protection against reactive oxygen species is provided by the copper containing enzyme superoxide dismutase 1 (SOD1). The copper chaperone CCS is responsible for copper insertion into apo-SOD1. This role is impaired by an interaction between the second PDZ domain (PDZ2α) of the neuronal adaptor protein X11α and the third domain of CCS (McLoughlin et al. (2001) J. Biol. Chem., 276, 9303–9307). The solution structure of the PDZ2α domain has been determined and the interaction with peptides derived from CCS has been explored. PDZ2α binds to the last four amino acids of the CCS protein (PAHL) with a dissociation constant of 91 ± 2 μM. Peptide variants have been used to map the interaction areas on PDZ2α for each amino acid, showing an important role for the C-terminal leucine, in line with canonical PDZ-peptide interactions.

Key words

complex NMR peptide SOD1 

Abbreviations

CCS

copper chaperone for SOD1

HOAc

acetic acid

PDZ

post-synaptic density 95, Drosophila disks-large, Zona occludens 1

RP-HPLC

reversed phase high-performance liquid chromatography

SOD1

superoxide dismutase 1

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Copyright information

© Springer 2005

Authors and Affiliations

  • Aude E. Duquesne
    • 1
  • Martina de Ruijter
    • 1
  • Jaap Brouwer
    • 1
  • Jan W. Drijfhout
    • 2
  • Sander B. Nabuurs
    • 3
  • Chris A. E. M. Spronk
    • 3
  • Geerten W. Vuister
    • 4
  • Marcellus Ubbink
    • 1
  • Gerard W. Canters
    • 1
  1. 1.Leiden Institute of ChemistryLeiden UniversityThe Netherlands
  2. 2.Department of Immunohematology and Blood TransfusionLeiden University Medical CenterLeidenThe Netherlands
  3. 3.CMBIRadboud UniversityNijmegenThe Netherlands
  4. 4.Department of Biophysical Chemistry, Institute for Molecules and MaterialsRadboud UniversityNijmegenThe Netherlands

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