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Publication Abstract from PubMed

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.

Structural characterization of the self-association domain of swallow.,Loening NM, Barbar E Protein Sci. 2021 Feb 27. doi: 10.1002/pro.4055. PMID:33641207^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.