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Article

The linker of des-Glu84-calmodulin is bent.

Proceedings of the National Academy of Sciences of the United States of America - 15 Jul 1993

Raghunathan S, Chandross R J, Cheng B P, Persechini A, Sobottka S E, Kretsinger R H

Abstract excerpt

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...

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Identifiers

PMID: 8341712
DOI: 10.1073/pnas.90.14.6869
PMCID: PMC47034

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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