 |
|
Title
|
|
The structure of apo-calmodulin. A 1H NMR examination of the carboxy-terminal domain.
|
|
|
Authors
|
|
B.E.Finn,
T.Drakenberg,
S.Forsén.
|
|
|
Ref.
|
|
FEBS Lett, 1993,
336,
368-374.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The structure of the carboxy-terminal domain of bovine calmodulin, TR2C, in the
calcium-free form was investigated using two-dimensional 1H NMR. Sequential
resonance assignments were made using standard methods. Using information from
medium and long range contacts revealed by nuclear Overhauser enhancement, the
secondary structure and global fold were determined. The apo protein possesses
essentially the same secondary structure as that in the calcium activated form
of intact calmodulin. However, the secondary structural elements are rearranged
so that the hydrophobic binding pocket is closed in the apo-form.
|
|
|
|