Departamento de Química Física Biológica, Instituto de Química Física Rocasolano, CSIC, Madrid, Spain.
FEBS Lett. 2011 Jan 3;585(1):53-7. doi: 10.1016/j.febslet.2010.11.027. Epub 2010 Nov 19.
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.
DYNLL1 是最小的动力蛋白轻链，与不同的货物相互作用，促进它们在细胞内的运输。通常，在目标中识别的序列与 GIQVD 或 KXTQT 基序同源，其中的谷氨酰胺对于结合很重要。在这里，我们添加了两个新的 DYNLL1 靶标，可以将它们分为这两类：ASFVP54 和神经胶质原纤维酸性蛋白。使用 NMR，我们证明了 DYNLL1 与两个源自其相互作用序列的肽之间的直接相互作用。我们对两个复合物的结构进行建模，并表明尽管在特定残基相互作用上存在差异，但整体结合模式与其他复合物保持一致。
