The structure of apo-calmodulin: A 1H NMR examination of the carboxy-terminal domain

B. Finn (Corresponding Author), Torbjörn Drakenberg, Sture Forsen

Research output: Contribution to journalArticleScientificpeer-review

33 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)368 - 373
Number of pages6
JournalFEBS Letters
Volume336
Issue number2
DOIs
Publication statusPublished - 1993
MoE publication typeA1 Journal article-refereed

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Calmodulin
Nuclear magnetic resonance
Calcium
Proteins
Proton Magnetic Resonance Spectroscopy

Cite this

Finn, B. ; Drakenberg, Torbjörn ; Forsen, Sture. / The structure of apo-calmodulin : A 1H NMR examination of the carboxy-terminal domain. In: FEBS Letters. 1993 ; Vol. 336, No. 2. pp. 368 - 373.
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The structure of apo-calmodulin : A 1H NMR examination of the carboxy-terminal domain. / Finn, B. (Corresponding Author); Drakenberg, Torbjörn; Forsen, Sture.

In: FEBS Letters, Vol. 336, No. 2, 1993, p. 368 - 373.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - The structure of apo-calmodulin

T2 - A 1H NMR examination of the carboxy-terminal domain

AU - Finn, B.

AU - Drakenberg, Torbjörn

AU - Forsen, Sture

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N2 - 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.

AB - 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.

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DO - 10.1016/0014-5793(93)80839-M

M3 - Article

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JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

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