Michaely P, Bennett V
Howard Hughes Medical Institute and Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
Trends Cell Biol. 1992 May;2(5):127-9. doi: 10.1016/0962-8924(92)90084-z.
Many proteins rely on stable, noncovalent interactions with other macromolecules to perform their function. The identification of a repeated sequence motif, the ANK repeat, in diverse proteins whose common function involves binding to other proteins indicates one way nature may achieve a wide range of protein-protein interactions. In this article, we describe evidence that these ANK repeats are involved in the specific recognition of proteins and possibly DNA, and present a model for the folding of the motif.
许多蛋白质依靠与其他大分子形成稳定的非共价相互作用来发挥其功能。在多种共同功能涉及与其他蛋白质结合的蛋白质中,发现了一种重复序列基序——锚蛋白重复序列(ANK重复序列),这表明自然界实现广泛蛋白质 - 蛋白质相互作用的一种方式。在本文中,我们描述了这些ANK重复序列参与蛋白质甚至可能是DNA的特异性识别的证据,并提出了该基序折叠的模型。