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Article

The structure of a calmodulin mutant with a deletion in the central helix: implications for molecular recognition and protein binding.

Structure (London, England : 1993) - 15 May 1997

Tabernero L, Taylor D A, Chandross R J, VanBerkum M F, Means A R, Quiocho F A, Sack J S

Abstract excerpt

BACKGROUND: Calmodulin (CaM) is the major calcium-dependent regulator of a large variety of important intracellular processes in eukaryotes. The structure of CaM consists of two globular calcium-binding domains joined by a central 28-residue alpha helix. This linker helix has been hypothesized to act as a flexible tether and is crucial for the binding and activation of numerous target proteins. Although the way...

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Identifiers

PMID: 9195880
DOI: 10.1016/s0969-2126(97)00217-7

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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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