Premium
The structure of apo‐calmodulin
Author(s) -
Finn Bryan E.,
Drakenberg Torbjörn,
Forsén Sture
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80839-m
Subject(s) - calmodulin , protein secondary structure , chemistry , calcium , ef hand , calcium binding protein , protein structure , biophysics , crystallography , biochemistry , biology , organic chemistry
The structure of the carboxy‐terminal domain of bovine calmodulin, TR 2 C, in the calcium‐free form was investigated using two‐dimensional 1 H 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.