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Structural models of DYNLL1 with interacting partners: African swine fever virus protein p54 and postsynaptic scaffolding protein gephyrin
Ist Teil von
FEBS letters, 2011-01, Vol.585 (1), p.53-57
Ort / Verlag
England: Elsevier B.V
Erscheinungsjahr
2011
Quelle
Wiley Online Library - AutoHoldings Journals
Beschreibungen/Notizen
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)