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
中科院分区:
文献类型:
--
作者:
吴更
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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DOI:
10.1038/7625
发表时间:
1999-04-01
期刊:
NATURE STRUCTURAL BIOLOGY
影响因子:
--
作者:
Kobe, B
通讯作者:
Kobe, B
影响因子:
16.8
作者:
Mitin, Natalia;Betts, Laurie;Rossman, Kent L.
通讯作者:
Rossman, Kent L.
影响因子:
8
作者:
Ritco-Vonsovici, Monica;Ababou, Abdessamad;Horton, Michael
通讯作者:
Horton, Michael
影响因子:
16
作者:
Y. Xing;W. Clements;I. Le Trong;T. Hinds;R. Stenkamp;D. Kimelman;Wenqing Xu
通讯作者:
Y. Xing;W. Clements;I. Le Trong;T. Hinds;R. Stenkamp;D. Kimelman;Wenqing Xu
影响因子:
16
作者:
Ha, NC;Tonozuka, T;Weis, WI
通讯作者:
Weis, WI