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Updated: Jun 6, 2026

Detection of In Situ Protein-protein Complexes at the Drosophila Larval Neuromuscular Junction Using Proximity Ligation Assay
Published on: January 20, 2015
Structural models of DYNLL1 with interacting partners: African swine fever virus protein p54 and postsynaptic
María Flor García-Mayoral1, I Rodríguez-Crespo, M Bruix
1Departamento de Química Física Biológica, Instituto de Química Física Rocasolano, CSIC, Madrid, Spain. mgarcia@iqfr.csic.es
Abstract:
DYNLL1, the smallest dynein light chain, interacts with different cargos facilitating their cellular transport. Usually the sequence recognized in the targets is homologous to the GIQVD or the KXTQT motifs with a glutamine that is important for binding. Here we add two new examples of DYNLL1 targets that can be classified into these two groups: ASFV p54 and gephyrin. Using NMR we demonstrate the direct interaction between DYNLL1 and two peptides derived from their interacting sequences. We model the structure of both complexes and show that the overall binding mode is preserved as in other complexes despite differences at the residue-specific interactions.
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