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1RGW

Solution Structure of ZASP's PDZ domain

Summary for 1RGW
Entry DOI10.2210/pdb1rgw/pdb
NMR InformationBMRB: 5696
DescriptorZASP protein (1 entity in total)
Functional Keywordszasp, pdz, cypher, oracle, muscle, z-disk, sarcomere, structural protein
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm, perinuclear region: O75112
Total number of polymer chains1
Total formula weight9149.41
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 citationAu, 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: 15062084
DOI: 10.1016/j.str.2004.02.019
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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