Structural models of DYNLL1 with interacting partners: African swine fever virus protein p54 and postsynaptic scaffolding protein gephyrin

• Published in: FEBS letters Vol. 585; no. 1; pp. 53 - 57
• Main Authors: García-Mayoral, María Flor, Rodríguez-Crespo, I., Bruix, M.
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 03.01.2011
• Subjects: African swine fever virus; African swine fever virus protein p54; Amino Acid Motifs; Amino Acid Sequence; Animals; Binding Sites - genetics; Carrier Proteins - chemistry; Carrier Proteins - metabolism; Cytoplasmic Dyneins - chemistry; Cytoplasmic Dyneins - metabolism; dynein ATPase; Dynein light chain; Gephyrin; glutamine; Humans; Magnetic Resonance Spectroscopy; Membrane Proteins - chemistry; Membrane Proteins - metabolism; Models, Molecular; Molecular Sequence Data; NMR; nuclear magnetic resonance spectroscopy; Oligopeptides - chemistry; Oligopeptides - metabolism; peptides; Protein Binding; protein structure; Protein Structure, Tertiary; Protein–protein interaction; scaffolding proteins; Sequence Homology, Amino Acid; Synapses - metabolism; viral proteins; Viral Structural Proteins - chemistry; Viral Structural Proteins - metabolism; Dynein light chain; African swine fever virus protein p54; NMR; Gephyrin; Protein–protein interaction
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/j.febslet.2010.11.027

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. MINT-8058152:DYNLL1 (uniprotkb:P63167) and gephyrin (uniprotkb:Q9NQX3) bind (MI:0407) by nuclear magnetic resonance (MI:0077) MINT-8058141:DYNLL1 (uniprotkb:P63167) and p54 (uniprotkb:Q4TWM1) bind (MI:0407) by nuclear magnetic resonance (MI:0077)