Crystal structure of the armadillo repeat domain of adenomatous polyposis coli which reveals its inherent flexibility.

Crystal structure of the armadillo repeat domain of adenomatous polyposis coli which reveals its inherent flexibility.
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腺瘤性息肉病大肠杆菌犰狳重复结构域的晶体结构揭示了其固有的灵活性。

DOI:
10.1016/j.bbrc.2011.08.044
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发表时间:
2011-09
影响因子:
3.1
通讯作者:
吴更
吴更
中科院分区:
生物学4区
文献类型:
--
作者:
吴更

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腺瘤性息肉病大肠杆菌 (APC) 蛋白的保守犰狳重复 (ARM) 结构域在识别其结合伴侣方面发挥着重要作用。在本研究中,我们报告了 APC-ARM(残基 407-775)的晶体结构,其分辨率为 2.9Å。我们的结构表明,APC-ARM 的七个犰狳重复折叠在一起形成一个紧凑的结构域,其中 Arm2 和 Arm5 与典型的犰狳重复存在一些偏差。 APC-ARM表面有一个带正电荷的凹槽,这可能是APC结合伙伴的识别位点。将该结构与我们之前报道的 APC (407-751) 结构进行比较,并结合正常模式分析,表明 APC-ARM 结构域具有有限的内在灵活性。我们认为这种内在的灵活性可能是 ARM 领域的固有属性。
The conserved armadillo repeat (ARM) domain of adenomatous polyposis coli (APC) protein plays an important role in the recognition of its binding partners. In this study, we report the crystal structure of APC-ARM (residues 407-775), which was determined to 2.9Å resolution. Our structure shows that the seven armadillo repeats of APC-ARM fold together into a compact domain, with Arm2 and Arm5 presenting some deviations from canonical armadillo repeats. There is a positively charged groove on the surface of APC-ARM, which might be the recognition site for APC-binding partners. Comparison of this structure with our previously reported structure of APC (407-751), together with normal mode analysis, reveals that the APC-ARM domain possesses a limited intrinsic flexibility. We propose that this intrinsic flexibility might be an inherent property of ARM domains in general.
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