Crystal Structure of a Tetradecameric Assembly of the Association Domain of Ca²⁺/Calmodulin-Dependent Kinase II
- Creators
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Hoelz, André
- Nairn, Angus C.
- Kuriyan, John
Abstract
We report the crystal structure of the 143 residue association domain of Ca²⁺/calmodulin-dependent protein kinase II (CaMKII). The association domain forms a hub-like assembly, composed of two rings of seven protomers each, which are stacked head to head and held together by extensive interfaces. The tetradecameric organization of the assembly was confirmed by analytical ultracentrifugation and multiangle light scattering. Individual protomers form wedge-shaped structures from which N-terminal helical segments that connect to the kinase domain extend toward the equatorial plane of the assembly, consistent with the arrangement of the kinase domains in a second outer ring. A deep and highly conserved pocket present within the association domain may serve as a docking site for proteins that interact with CaMKII.
Additional Information
© 2003 Cell Press. Published by Elsevier Inc. Received 12 December 2002, Revised 3 March 2003, Accepted 7 March 2003. We thank R. Colbran for the gift of a mouse CaMKIIα cDNA clone, G. Schneider and S.A. Darst for the gift of various cluster compounds, H. Viguette for technical assistance with Sf9 cell expression, S. Ray for mass spectrometric analysis, N. Rodionova for technical assistance with ultracentrifugation experiments, B. Nagar and J.B. Bonanno for help with crystallography, H. Sondermann for help with multiangle light-scattering experiments, B. Corwin for help with crystallization, and T. Sakmar and G. Blobel for sharing laboratory resources and support. The schematic illustrations in Figure 5 were drawn by Lore Leighton. We are indebted to Thomas Earnest, Gerry McDermott, and the scientific staff of the Advanced Light Source (ALS), LBNL, for assistance in the collection of diffraction data. Additional thanks go to members of the Kuriyan, Burley, Sakmar, and Blobel labs for many helpful suggestions and discussions. N-terminal protein sequencing and DNA sequencing were performed by the Protein/DNA Technology Center of the Rockefeller University. A.H. was supported by the Burroughs Wellcome Fund Interfaces in Science program. Accession Numbers: The coordinates of the structure have been deposited in the Protein Data Bank (accession number 1HKX).Attached Files
Supplemental Material - 1-s2.0-S1097276503001710-mmc1.jpg
Supplemental Material - 1-s2.0-S1097276503001710-mmc2.jpg
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Additional details
- Eprint ID
- 102386
- Resolver ID
- CaltechAUTHORS:20200407-124429627
- Burroughs Wellcome Fund
- Created
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2020-04-07Created from EPrint's datestamp field
- Updated
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2021-11-16Created from EPrint's last_modified field