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. 1993 Jul 15;90(14):6869–6873. doi: 10.1073/pnas.90.14.6869

The linker of des-Glu84-calmodulin is bent.

S Raghunathan 1, R J Chandross 1, B P Cheng 1, A Persechini 1, S E Sobottka 1, R H Kretsinger 1
PMCID: PMC47034  PMID: 8341712

Abstract

The crystal structure of a mutant calmodulin (CaM) lacking Glu-84 has been refined to R = 0.23 using data measured to 2.9-A resolution. In native CaM the central helix is fully extended, and the molecule is dumbbell shaped. In contrast, the deletion of Glu-84 causes a bend of 95 degrees in the linker region of the central helix at Ile-85. However, EF-hand domains 1 and 2 (lobe 1,2) do not touch lobe 3,4. The length, by alpha-carbon separation, of des-Glu84-CaM is 56 A; that of native CaM is 64 A. The shape of des-Glu84-CaM is similar to that of native CaM, as it is bound to the target peptide of myosin light-chain kinase. This result supports the proposal that the linker region of the central helix of CaM functions as a flexible tether.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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