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首页> 外文期刊>Journal of Molecular Biology >Crystal structure of the amino-terminal coiled-coil domain of the APC tumor suppressor.
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Crystal structure of the amino-terminal coiled-coil domain of the APC tumor suppressor.

机译：APC肿瘤抑制因子氨基末端卷曲螺旋结构域的晶体结构。

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摘要

Coiled coils serve as dimerization domains for a wide variety of proteins, including the medically important oligomeric tumor suppressor protein, APC. Mutations in the APC gene are associated with an inherited susceptibility to colon cancer and with approximately 75 % of sporadic colorectal tumors. To define the basis for APC pairing and to explore the anatomy of dimeric coiled coils, we determined the 2.4 A resolution X-ray crystal structure of the N-terminal dimerization domain of APC. The peptide APC-55, encompassing the heptad repeats in APC residues 2-55, primarily forms an alpha-helical, coiled-coil dimer with newly observed core packing features. Correlated asymmetric packing of four core residues in distinct, standard rotamers is associated with a small shift in the helix register. At the C terminus, the helices splay apart and interact with a symmetry-related dimer in the crystal to form a short, anti-parallel, four-helix bundle. N-terminal fraying and C-terminal splaying of the helices, as well as the asymmetry and helix register shift describe unprecedented dynamic excursions of coiled coils. The low stability of APC-55 and divergence from the expected coiled-coil fold support the suggestion that the APC dimerization domain may extend beyond the first 55 residues. Copyright 2000 Academic Press.
机译：螺旋线圈用作多种蛋白质的二聚化结构域，包括医学上重要的寡聚肿瘤抑制蛋白APC。 APC基因中的突变与结肠癌的遗传易感性以及约75％的散发性结直肠肿瘤有关。为了定义APC配对的基础并探索二聚体螺旋线圈的解剖结构，我们确定了APC N端二聚化域的2.4 A分辨率X射线晶体结构。肽APC-55包含APC残基2-55中的七肽重复序列，主要形成具有新观察到的核心堆积特征的α-螺旋，卷曲螺旋二聚体。不同的标准旋转异构体中四个核心残基的相关不对称堆积与螺旋寄存器中的小位移相关。在C末端，螺旋彼此分开，并与晶体中与对称相关的二聚体相互作用，形成一个短的，反平行的四螺旋束。螺旋的N端磨损和C端张开，以及不对称和螺旋寄存器偏移描述了线圈的空前动态变化。 APC-55的低稳定性和与预期的卷曲螺旋折叠的背离证明了APC二聚结构域可能会延伸到前55个残基之外。版权所有2000学术出版社。

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