Ca2+-independent binding of an EF-hand domain to a novel motif in the alpha-actinin-titin complex.
Copyright policy )Ca2+-independent binding of an EF-hand domain to a novel motif in the alpha-actinin-titin complex.
The interaction between alpha-actinin and titin, two modular muscle proteins, is essential for sarcomere assembly. We have solved the solution structure of a complex between the calcium-insensitive C-terminal EF-hand domain of alpha-actinin-2 and the seventh Z-repeat of titin. The structure of the complex is in a semi-open conformation and closely resembles that of myosin light chains in their complexes with heavy chain IQ motifs. However, no IQ motif is present in the Z-repeat, suggesting that the semi-open conformation is a general structural solution for calcium-independent recognition of EF-hand domains.
- University of Pavia Italy
- University of Leicester United Kingdom
- Scuola Normale Superiore Italy
- NIHR Biomedical Research Centre at The Royal Marsden and the ICR United Kingdom
Models, Molecular, 570, Binding Sites, Sequence Homology, Amino Acid, Protein Conformation, Nuclear Magnetic Resonance, Amino Acid Motifs, Calcium-Binding Proteins, Molecular Sequence Data, Molecular, Sequence Homology, Muscle Proteins, 540, Amino Acid, Models, Actinin, Calcium, Connectin, Amino Acid Sequence, Nuclear Magnetic Resonance, Biomolecular, Protein Kinases, Biomolecular
Models, Molecular, 570, Binding Sites, Sequence Homology, Amino Acid, Protein Conformation, Nuclear Magnetic Resonance, Amino Acid Motifs, Calcium-Binding Proteins, Molecular Sequence Data, Molecular, Sequence Homology, Muscle Proteins, 540, Amino Acid, Models, Actinin, Calcium, Connectin, Amino Acid Sequence, Nuclear Magnetic Resonance, Biomolecular, Protein Kinases, Biomolecular
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