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PDBsum entry 1rgw
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Structural protein
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PDB id
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1rgw
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Solution structure of zasp pdz domain; implications for sarcomere ultrastructure and enigma family redundancy.
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Authors
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Y.Au,
R.A.Atkinson,
R.Guerrini,
G.Kelly,
C.Joseph,
S.R.Martin,
F.W.Muskett,
A.Pallavicini,
G.Faulkner,
A.Pastore.
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Ref.
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Structure, 2004,
12,
611-622.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 1.
Figure 1. Diagram of the Sarcomere and Domain
Architecture(A) Schematic representation of the sarcomere. The
position of the Z disk and of the M line is indicated. A single
molecule titin filament (indicated in green) connects the Z disk
to the M line. In the Z disk, a-actinin-2 (in yellow) forms
transversal connections between actin filaments (in red) and is
thought to bind ZASP (in blue).(B) Domain architecture of the
titin region localized in the Z disk, a-actinin-2, and ZASP
(variant 3).
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2004,
12,
611-622)
copyright 2004.
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