Crystal structure of apo-calmodulin bound to the first two IQ motifs of myosin V reveals essential recognition features
A 2.5-Å resolution structure of calcium-free calmodulin (CaM) bound to the first two IQ motifs of the murine myosin V heavy chain reveals an unusual CaM conformation. The C-terminal lobe of each CaM adopts a semi-open conformation that grips the first part of the IQ motif (IQxxxR), whereas the N-ter...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2006-12, Vol.103 (51), p.19326-19331 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Houdusse, Anne Gaucher, Jean-François Krementsova, Elena Mui, Suet Trybus, Kathleen M Cohen, Carolyn |
| description | A 2.5-Å resolution structure of calcium-free calmodulin (CaM) bound to the first two IQ motifs of the murine myosin V heavy chain reveals an unusual CaM conformation. The C-terminal lobe of each CaM adopts a semi-open conformation that grips the first part of the IQ motif (IQxxxR), whereas the N-terminal lobe adopts a closed conformation that interacts more weakly with the second part of the motif (GxxxR). Variable residues in the IQ motif play a critical role in determining the precise structure of the bound CaM, such that even the consensus residues of different motifs show unique interactions with CaM. This complex serves as a model for the lever arm region of many classes of unconventional myosins, as well as other IQ motif-containing proteins such as neuromodulin and IQGAPs. |
| doi_str_mv | 10.1073/pnas.0609436103 |
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The C-terminal lobe of each CaM adopts a semi-open conformation that grips the first part of the IQ motif (IQxxxR), whereas the N-terminal lobe adopts a closed conformation that interacts more weakly with the second part of the motif (GxxxR). Variable residues in the IQ motif play a critical role in determining the precise structure of the bound CaM, such that even the consensus residues of different motifs show unique interactions with CaM. 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| subjects | Amino Acid Motifs - genetics Animals Arm Binding sites Biological Sciences Calcium Calmodulin - chemistry Calmodulin - metabolism Cloning, Molecular Consensus sequence Crystal structure Crystallization Drug interactions Hydrogen bonds Mice Models, Molecular Molecules Myosin Type V - chemistry Myosin Type V - metabolism Protein Binding Protein Conformation Proteins |
| title | Crystal structure of apo-calmodulin bound to the first two IQ motifs of myosin V reveals essential recognition features |
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