The FP Domains of PI31 and Fbxo7 have the same Protein Fold but very Different Modes of Protein–Protein Interaction
The FP Domains of PI31 and Fbxo7 have the same Protein Fold but very Different Modes of Protein–Protein Interaction
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PI31 和 Fbxo7 的 FP 结构域具有相同的蛋白质折叠，但蛋白质-蛋白质相互作用的模式截然不同
DOI：
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发表时间：
2015
影响因子：
4.4
通讯作者：
Z. Du
中科院分区：
文献类型：
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作者：
J. Shang;Xiaolan Huang;Z. Du
Fbxo 7和PI 31含有介导蛋白质的同源/异源二聚化的保守FP结构域。PI 31 FP结构域还可以与Fbxo 7中的F盒基序相互作用。FP结构域介导的蛋白质-蛋白质相互作用对于Fbxo 7和PI 31的功能是重要的。先前确定了Fbxo 7和PI 31 FP结构域的晶体结构，表明Fbxo 7 FP结构域中的C-末端螺旋不存在于PI 31 FP结构域中。在这里，我们使用更长的蛋白质构建体确定PI 31 FP结构域的晶体结构。该结构与Fbxo 7 FP结构域（包括C-末端螺旋）相当，表明两个FP结构域共享相同的全局折叠。然而，FP结构域也具有其自身的结构特征，主要是在最长的环（由于广泛的氢键和疏水相互作用，其具有很大程度上固定的构象）和C-末端区域。晶体结构还揭示了由两个FP结构域介导的蛋白质-蛋白质相互作用模式的根本差异：PI 31 FP结构域利用α界面或β界面进行同二聚体相互作用，而Fbxo 7 FP结构域利用αβ界面。我们进行建模研究表明，域特定的结构特征可能会决定域间的相互作用的特定模式。我们提出异二聚体相互作用将由分别由Fbxo 7和PI 31 FP结构域的α-螺旋和β-折叠表面组成的αβ界面介导。我们还讨论了FP结构域介导的蛋白质-蛋白质相互作用的各种模式的结构/功能意义。
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 α interface or β interface for homodimeric interaction, whereas the Fbxo7 FP domain utilizes an αβ 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 αβ interface consisting of the α-helical and β-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.
影响因子：
16
作者：
Hao, Bing;Oehlmann, Stephanie;Pavletich, Nikola P.
通讯作者：
Pavletich, Nikola P.
用于自动确定大分子结构的Phenix软件。
影响因子：
4.8
作者：
Adams, Paul D.;Afonine, Pavel V.;Bunkoczi, Gabor;Chen, Vincent B.;Echols, Nathaniel;Headd, Jeffrey J.;Hung, Li-Wei;Jain, Swati;Kapral, Gary J.;Kunstleve, Ralf W. Grosse;McCoy, Airlie J.;Moriarty, Nigel W.;Oeffner, Robert D.;Read, Randy J.;Richardson, David C.;Richardson, Jane S.;Terwilliger, Thomas C.;Zwart, Peter H.
通讯作者：
Zwart, Peter H.
影响因子：
11.8
作者：
Zeng Z;Wang W;Yang Y;Chen Y;Yang X;Diehl JA;Liu X;Lei M
通讯作者：
Lei M