Abstract
We have determined the crystal structure of the two central repeats in the alpha-actinin rod at 2.5 A resolution. The repeats are connected by a helical linker and form a symmetric, antiparallel dimer in which the repeats are aligned rather than staggered. Using this structure, which reveals the structural principle that governs the architecture of alpha-actinin, we have devised a plausible model of the entire alpha-actinin rod. The electrostatic properties explain how the two alpha-actinin subunits assemble in an antiparallel fashion, placing the actin-binding sites at both ends of the rod. This molecular architecture results in a protein that is able to form cross-links between actin filaments.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Actin Cytoskeleton / chemistry*
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Actins / chemistry*
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Amino Acid Sequence
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Connectin
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Crystallography, X-Ray
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Cytoskeletal Proteins
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Dimerization
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Glycoproteins
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Humans
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Macromolecular Substances
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Metalloproteins / chemistry
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Models, Molecular
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Molecular Sequence Data
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Muscle Proteins / chemistry
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Protein Conformation*
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Protein Kinases / chemistry
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Protein Structure, Secondary
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Recombinant Fusion Proteins / chemistry
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Repetitive Sequences, Amino Acid*
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Sequence Alignment
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Spectrin / chemistry
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Static Electricity
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Structure-Activity Relationship
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Talin / chemistry
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Vinculin / chemistry
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Zyxin
Substances
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Actins
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Connectin
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Cytoskeletal Proteins
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Glycoproteins
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Macromolecular Substances
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Metalloproteins
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Muscle Proteins
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Recombinant Fusion Proteins
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TTN protein, human
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Talin
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ZYX protein, human
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Zyxin
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Vinculin
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Spectrin
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Protein Kinases