1y7n
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(New page: 200px<br /> <applet load="1y7n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y7n" /> '''Solution structure of the second PDZ domain...)
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Revision as of 18:09, 12 November 2007
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Solution structure of the second PDZ domain of the human neuronal adaptor X11alpha
Overview
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 (PDZ2alpha) of the, neuronal adaptor protein X11alpha and the third domain of CCS (McLoughlin, et al. (2001) J. Biol. Chem., 276, 9303-9307). The solution structure of, the PDZ2alpha domain has been determined and the interaction with peptides, derived from CCS has been explored. PDZ2alpha binds to the last four amino, acids of the CCS protein (PAHL) with a dissociation constant of 91 +/- 2, microM. Peptide variants have been used to map the interaction areas on, PDZ2alpha for each amino acid, showing an important role for the, C-terminal leucine, in line with canonical PDZ-peptide interactions.
About this Structure
1Y7N is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of the second PDZ domain of the neuronal adaptor X11alpha and its interaction with the C-terminal peptide of the human copper chaperone for superoxide dismutase., Duquesne AE, Ruijter M, Brouwer J, Drijfhout JW, Nabuurs SB, Spronk CA, Vuister GW, Ubbink M, Canters GW, J Biomol NMR. 2005 Jul;32(3):209-18. PMID:16132821
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