1Y7N

Solution structure of the second PDZ domain of the human neuronal adaptor X11alpha

Summary for 1Y7N

• Entry DOI: 10.2210/pdb1y7n/pdb
• Descriptor: Amyloid beta A4 precursor protein-binding family A member 1 (1 entity in total)
• Functional Keywords: copper chaperone for superoxide dismutase, neuronal adaptor, protein transport
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 9933.56

Authors

Duquesne, A.E.,de Ruijter, M.,Brouwer, J.,Drijfhout, J.W.,Nabuurs, S.B.,Spronk, C.A.E.M.,Vuister, G.W.,Ubbink, M.,Canters, G.W. (deposition date: 2004-12-09, release date: 2005-11-22, Last modification date: 2024-05-29)

Primary citation

Duquesne, A.E.,de Ruijter, M.,Brouwer, J.,Drijfhout, J.W.,Nabuurs, S.B.,Spronk, C.A.E.M.,Vuister, G.W.,Ubbink, M.,Canters, G.W.
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
J.Biomol.Nmr, 32:209-218, 2005

PubMed 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 (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.

PubMed: 16132821
DOI: 10.1007/s10858-005-7333-1

Experimental method

SOLUTION NMR