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Structural characterization of the self-association domain of swallow.

ABSTRACT: Swallow, a 62 kDa multidomain protein, is required for the proper localization of several mRNAs involved in the development of Drosophila oocytes. The dimerization of Swallow depends on a 71-residue self-association domain in the center of the protein sequence, and is significantly stabilized by a binding interaction with dynein light chain (LC8). Here, we detail the use of solution-state nuclear magnetic resonance spectroscopy to characterize the structure of this self-association domain, thereby establishing that this domain forms a parallel coiled-coil and providing insight into how the stability of the dimerization interaction is regulated.

SUBMITTER: Loening NM

PROVIDER: S-EPMC8040862 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature

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Structural characterization of the self-association domain of swallow.

Loening Nikolaus M NM Barbar Elisar E

Protein science : a publication of the Protein Society 20210309 5

Swallow, a 62 kDa multidomain protein, is required for the proper localization of several mRNAs involved in the development of Drosophila oocytes. The dimerization of Swallow depends on a 71-residue self-association domain in the center of the protein sequence, and is significantly stabilized by a binding interaction with dynein light chain (LC8). Here, we detail the use of solution-state nuclear magnetic resonance spectroscopy to characterize the structure of this self-association domain, there ...[more]

PMID: 33641207

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