Abstract
We have determined the solution structures of the apo and (Ca2+)(2) forms of the carboxy-terminal domain of calmodulin using multidimensional heteronuclear nuclear magnetic resonance spectroscopy, The results show that both forms adopt well-defined structures with essentially equal secondary structure, A comparison of the structures of the two forms shows that Ca2+ binding causes major rearrangements of the secondary structure elements with changes in inter-residue distances of up to 15 Angstrom and exposure of the hydrophobic interior of the four-helix bundle, Comparisons with previously determined high-resolution X-ray structures and models of calmodulin indicate that this domain is structurally autonomous.
| Original language | English |
|---|---|
| Pages (from-to) | 777-783 |
| Number of pages | 7 |
| Journal | Nature Structural Biology |
| Volume | 2 |
| Issue number | 9 |
| DOIs | |
| Publication status | Published - 1995 |
| Externally published | Yes |
Cite this
- APA
- Author
- BIBTEX
- Harvard
- Standard
- RIS
- Vancouver