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首页> 外文期刊>Journal of Biomolecular Structure and Dynamics >The FP domains of PI31 and Fbxo7 have the same protein fold but very different modes of protein-protein interaction
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The FP domains of PI31 and Fbxo7 have the same protein fold but very different modes of protein-protein interaction

机译：PI31和FBXO7的FP结构域具有相同的蛋白质折叠，但蛋白质 - 蛋白质相互作用的非常不同的模式

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摘要

Fbxo7 and PI31 contain a conserved FP domain that mediates the homo-/hetero-dimerization of the proteins. The PI31 FP domain may also interact with the F-box motif in Fbxo7. The FP domain-mediated protein-protein interactions are important for the functions of Fbxo7 and PI31. The crystal structures of the Fbxo7 and PI31 FP domains were determined previously, showing that a C-terminal helix in the Fbxo7 FP domain was not present in the PI31 FP domain. Here, we determine the crystal structure of the PI31 FP domain using a longer protein construct. The structure is comparable to the Fbxo7 FP domain (including the C-terminal helix), indicating that the two FP domains share the same global fold. However, the FP domains also harbor their own characteristic structural features, mainly in the longest loop (which has a largely fixed conformation due to extensive hydrogen bonding and hydrophobic interactions) and the C-terminal end regions. The crystal structures also reveal fundamental differences in the modes of protein-protein interactions mediated by the two FP domains: the PI31 FP domain utilizes either an alpha interface or beta interface for homodimeric interaction, whereas the Fbxo7 FP domain utilizes an alpha beta interface. We perform modeling studies to show that the domain-specific structural features may dictate specific modes of inter-domain interactions. We propose that a heterodimeric interaction would be mediated by an alpha beta interface consisting of the alpha-helical and beta-sheet surfaces of the Fbxo7 and PI31 FP domains, respectively. We also discuss the structural/functional significance of various modes of FP domain-mediated protein-protein interactions.
机译：FBXO7和PI31含有保守的FP结构域，介导蛋白质的均匀/杂二聚化。 PI31 FP域还可以在FBXO7中与F-Box图案相互作用。 FP结构域介导的蛋白质 - 蛋白质相互作用对于FBXO7和PI31的功能很重要。先前确定FBXO7和PI31 FP结构域的晶体结构，表明FBXO7 FP结构域中的C末端螺旋不存在于PI31 FP结构域中。这里，我们使用更长的蛋白质构建体确定PI31 FP结构域的晶体结构。该结构与FBXO7 FP域（包括C终端螺旋）相当，表明两个FP域共享相同的全局折叠。然而，FP结构域还涉及自己的特征结构特征，主要是在最长的环（由于广泛的氢键和疏水相互作用而具有很大的固定构象）和C末端端区域。晶体结构还揭示了两种FP结构域介导的蛋白质 - 蛋白质相互作用模式的基本差异：PI31 FP域利用α接口或β接口进行同型二聚体交互，而FBXO7 FP域利用Alphaβ接口。我们进行建模研究以表明域特定的结构特征可以决定域间交互的特定模式。我们提出，异细化相互作用将由由FBXO7和PI31 FP结构域的α-螺旋和β-片表面组成的αβ界面介导。我们还讨论了各种FP域介导的蛋白质 - 蛋白质相互作用的结构/功能意义。

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