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Title: Solution structure of ZASP PDZ domain; implications for sarcomere ultrastructure and enigma family redundancy.
Authors: Au, Y
Atkinson, RA
Guerrini, R
Kelly, G
Joseph, C
Martin, SR
Muskett, FW
Pallavicini, A
Faulkner, G
Pastore, A
First Published: Apr-2004
Citation: STRUCTURE, 2004, 12 (4), pp. 611-622
Abstract: Z band alternately spliced PDZ-containing protein (ZASP) is a sarcomere Z disk protein expressed in human cardiac and skeletal muscle that is thought to be involved in a dominant familial dilated cardiomyopathy. The N-terminal PDZ domain of ZASP interacts with the C terminus of alpha-actinin-2, the major component of the Z disk, probably by forming a ternary complex with titin Z repeats. We have determined the structure of ZASP PDZ by NMR and showed that it is a classical class 1 PDZ domain that recognizes the carboxy-terminal sequence of an alpha-actinin-2 calmodulin-like domain with micromolar affinity. We also characterized the role of each component in the ternary complex ZASP/alpha-actinin-2/titin, showing that the alpha-actinin-2/ZASP PDZ interaction involves a binding surface distinct from that recognized by the titin Z repeats. ZASP PDZ structure was used to model other members of the enigma family by homology and to predict their abilities to bind alpha-actinin-2.
DOI Link: 10.1016/j.str.2004.02.019
ISSN: 0969-2126
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

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