6XOR

Structure of the Self-Association Domain of Swallow

Summary for 6XOR

Entry DOI	10.2210/pdb6xor/pdb
Related	3E2B
NMR Information	BMRB: 30768
Descriptor	Protein swallow (1 entity in total)
Functional Keywords	coiled coil, self-association domain, rna binding protein
Biological source	Drosophila melanogaster (Fruit fly)
Total number of polymer chains	2
Total formula weight	17118.93
Authors	Loening, N.M.,Barbar, E. (deposition date: 2020-07-07, release date: 2021-03-24, Last modification date: 2024-05-15)
Primary citation	Loening, N.M.,Barbar, E. Structural characterization of the self-association domain of swallow. Protein Sci., 30:1056-1063, 2021 Cited by PubMed 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. PubMed: 33641207 DOI: 10.1002/pro.4055 PDB entries with the same primary citation
Experimental method	SOLUTION NMR

Structure validation