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首页> 外文期刊>Acta crystallographica. Section D, Structural biology. >Crystal structure of the PEG‐bound SH3 domain of myosin IB from Entamoeba histolytica Entamoeba histolytica reveals its mode of ligand recognition
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Crystal structure of the PEG‐bound SH3 domain of myosin IB from Entamoeba histolytica Entamoeba histolytica reveals its mode of ligand recognition

机译：晶体结构的束缚SH3域等挂钩阿米巴揭示其配体的模式识别

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摘要

The versatility in the recognition of various interacting proteins by the SH3 domain drives a variety of cellular functions. Here, the crystal structure of the C‐terminal SH3 domain of myosin IB from Entamoeba histolytica ( Eh MySH3) is reported at a resolution of 1.7?? in native and PEG‐bound states. Comparisons with other structures indicated that the PEG molecules occupy protein–protein interaction pockets similar to those occupied by the peptides in other peptide‐bound SH3‐domain structures. Also, analysis of the PEG‐bound Eh MySH3 structure led to the recognition of two additional pockets, apart from the conventional polyproline and specificity pockets, that are important for ligand interaction. Molecular‐docking studies combined with various comparisons revealed structural similarity between Eh MySH3 and the SH3 domain of β‐Pix, and this similarity led to the prediction that Eh MySH3 preferentially binds targets containing type II‐like P XX P motifs. These studies expand the understanding of the Eh MySH3 domain and provide extensive structural knowledge, which is expected to help in predicting the interacting partners which function together with myosin IB during phagocytosis in E. histolytica infections.
机译：识别不同的多功能性相互作用的蛋白质的SH3域驱动各种各样的细胞功能。C的结构检测终端SH3肌凝蛋白的领域报道的分辨率1.7 ? ?挂钩的绑定状态。结构表明,PEG分子占领口袋蛋白质间交互作用类似的肽其他肽量约束SH3域结构。分析领导挂钩绑定呃MySH3应承担的结构识别的两个额外的口袋,除了传统的polyproline和特异性的口袋,这是很重要的配位体的相互作用。结合各种比较结构相似性呃MySH3和SH3β域高焦油和这种相似性导致嗯MySH3优先结合的预测目标包含II型类P XX P图案。这些研究扩大的理解是吧MySH3域和提供广泛的结构知识,这将帮助预测的互动合作伙伴函数与肌球蛋白IB期间吞噬作用在大肠阿米巴感染。

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