Supercoiled protein motifs:: The collagen triple-helix and the α-helical coiled coil
Supercoiled protein motifs:: The collagen triple-helix and the α-helical coiled coil
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DOI：
10.1006/jsbi.1998.3965
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发表时间：
1998-01-01
影响因子：
3
通讯作者：
Brodsky, B
中科院分区：
文献类型：
--
作者：
Beck, K;Brodsky, B
胶原蛋白的三螺旋结构和α -螺旋螺旋结构代表了两种基本的超螺旋多链蛋白基序。最初，它们以纤维蛋白为特征，但最近在许多其他含有棒状结构域的蛋白质中发现了它们。螺旋结构域负责蛋白质的寡聚化以及其他特定功能，而三螺旋结构域则形成超分子结构并结合各种配体。这两种结构最初都是通过纤维衍射来解决的，最近对小蛋白质和肽模型的晶体学研究证实了这种结构并提供了分子细节。讨论了这两种基序分子构象的差异以及稳定这些构象的相互作用。这两个基序的分子结构将氨基酸序列限制为可识别的模式，胶原蛋白三螺旋结构需要（Gly-X-Y）(n)重复序列，而螺旋结构域则需要不那么严格的七核苷酸重复要求（h-x-x-h-x-x-x -x）(n)，其中h代表疏水残基。当这些超螺旋结构域在同一蛋白质中相邻时，就会考虑它们在蛋白质中的特征和作用。(C) 1998学术出版社。
The collagen triple-helix and the alpha-helical coiled coil represent the two basic supercoiled multi-stranded protein motifs. Originally they were characterized in fibrous proteins, but have been found more recently in a number of other proteins containing rod-shaped domains. Coiled-coil domains are responsible for the oligomerization of proteins, as well as other specific functions, while the triple-helix domains associate to form supramolecular structures and bind a variety of ligands. Both structures were originally solved by fiber diffraction, and recent crystallographic studies on small proteins and peptide models have confirmed the structure and provided molecular details. The differences in the molecular conformations of these two motifs and the interactions stabilizing these conformations are discussed. The molecular structures of both motifs constrain the amino acid sequence to recognizable patterns, requiring the (Gly-X-Y)(n) repeating sequence for the collagen triple-helix and a less stringent heptad repeat requirement (h-x-x-h-x-x-x)(n) for the coiled-coil domains, where h represents hydrophobic residues. The features and roles of these supercoiled domains in proteins are considered when they are found adjacent in the same protein. (C) 1998 Academic Press.