1RGW
Solution Structure of ZASP's PDZ domain
Summary for 1RGW
Entry DOI | 10.2210/pdb1rgw/pdb |
NMR Information | BMRB: 5696 |
Descriptor | ZASP protein (1 entity in total) |
Functional Keywords | zasp, pdz, cypher, oracle, muscle, z-disk, sarcomere, structural protein |
Biological source | Homo sapiens (human) |
Cellular location | Cytoplasm, perinuclear region: O75112 |
Total number of polymer chains | 1 |
Total formula weight | 9149.41 |
Authors | Au, Y.,Atkinson, R.A.,Pallavicini, A.,Joseph, C.,Martin, S.R.,Muskett, F.W.,Guerrini, R.,Faulkner, G.,Pastore, A. (deposition date: 2003-11-13, release date: 2004-04-13, Last modification date: 2024-05-22) |
Primary citation | Au, Y.,Atkinson, R.A.,Guerrini, R.,Kelly, G.,Joseph, C.,Martin, S.R.,Muskett, F.W.,Pallavicini, A.,Faulkner, G.,Pastore, A. Solution Structure of ZASP PDZ Domain; Implications for Sarcomere Ultrastructure and Enigma Family Redundancy. Structure, 12:611-622, 2004 Cited by PubMed 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. PubMed: 15062084DOI: 10.1016/j.str.2004.02.019 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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