X-ray analysis reveals conformational adaptation of the linker in functional calmodulin mutants

Crystal structures of target peptide bound Ca 2+ -calmodulin linker helix mutants with the helix shortened by two or three residues, or replaced by the longer troponin C central helix, show that the major calmodulin-target structure is preserved at the expense of linker conformation.

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Bibliographische Detailangaben
Veröffentlicht in:	Nature Structural Biology 1995-11, Vol.2 (11), p.943-945
Hauptverfasser:	Meador, William E., George, Samuel E., Means, Anthony R., Quiocho, Florante A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Biochemistry Biological Microscopy Biomedical and Life Sciences Calcium-Calmodulin-Dependent Protein Kinase Type 2 Calcium-Calmodulin-Dependent Protein Kinases - chemistry Calcium-Calmodulin-Dependent Protein Kinases - metabolism Calmodulin - chemistry Calmodulin - genetics Calmodulin - metabolism correspondence Crystallography, X-Ray Life Sciences Membrane Biology Models, Molecular Mutation Protein Binding Protein Structure
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Beschreibung
Zusammenfassung:	Crystal structures of target peptide bound Ca 2+ -calmodulin linker helix mutants with the helix shortened by two or three residues, or replaced by the longer troponin C central helix, show that the major calmodulin-target structure is preserved at the expense of linker conformation.
ISSN:	1072-8368 1545-9993 1545-9985
DOI:	10.1038/nsb1195-943