Solution structure of the second PDZ domain of the
neuronal adaptor X11a and its interaction with the
C-terminal peptide of the human copper chaperone for
superoxide dismutase
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 (PDZ2a) of
the neuronal adaptor protein X11a and the third domain of
CCS (McLoughlin et al. (2001) J. Biol. Chem., 276,
9303–9307). The solution structure of the PDZ2a
domain has been determined and the interaction with
peptides derived from CCS has been explored. PDZ2a binds to
the last four amino acids of the CCS protein (PAHL) with a
dissociation constant of 91 ± 2 uM. Peptide variants have
been used to map the interaction areas on PDZ2a for each
amino acid, showing an important role for the C-terminal
leucine, in line with canonical PDZ-peptide interactions.
PDB code 1Y7N. (
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■ Aude E. Duquesne, Martina de Ruijter, Jaap Brouwer,
Jan W. Drijfhoutb, Sander B. Nabuurs, Chris A. E. M.
Spronk, Geerten W. Vuister, Marcellus Ubbink & Gerard
W. Canters (2005) "Solution structure of the second PDZ
domain of the neuronal adaptor X11a and its interaction
with the C-terminal peptide of the human copper chaperone
for superoxide dismutase"
J. Biomol. NMR
32, 209-218.
