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首页> 外文期刊>Journal of Molecular Biology >Stereospecific interactions of proline residues in protein structures and complexes.
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Stereospecific interactions of proline residues in protein structures and complexes.

机译：脯氨酸残基在蛋白质结构和复合物中的立体特异性相互作用。

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摘要

The constrained backbone torsion angle of a proline (Pro) residue has usually been invoked to explain its three-dimensional context in proteins. Here we show that specific interactions involving the pyrrolidine ring atoms also contribute to its location in a given secondary structure and its binding to another molecule. It is adept at participating in two rather non-conventional interactions, C-H...pi and C-H...O. The geometry of interaction between the pyrrolidine and aromatic rings, vis-a-vis the occurrence of the C-H...pi interactions has been elucidated. Some of the secondary structural elements stabilized by Pro-aromatic interactions are beta-turns, where a Pro can interact with an adjacent aromatic residue, and in antiparallel beta-sheet, where a Pro in an edge strand can interact with an aromatic residue in the adjacent strand at a non-hydrogen-bonded site. The C-H groups at the Calpha and Cdelta positions can form strong C-H...O interactions (as seen from the clustering of points) and such interactions involving a Pro residue at C' position relative to an alpha-helix can cap the hydrogen bond forming potentials of the free carbonyl groups at the helix C terminus. Functionally important Pro residues occurring at the binding site of a protein almost invariably engage aromatic residues (with one of them being held by C-H...pi interaction) from the partner molecule in the complex, and such aromatic residues are highly conserved during evolution.
机译：通常调用脯氨酸（Pro）残基的受约束主链扭转角来解释其在蛋白质中的三维背景。在这里，我们表明涉及吡咯烷环原子的特定相互作用也有助于其在给定二级结构中的位置以及与另一分子的结合。它善于参与两个非常常规的交互，C-H ... pi和C-H ... O。已经阐明了吡咯烷与芳环之间相互作用的几何形状，相对于C-H ... pi相互作用的发生。通过Pro-芳香族相互作用稳定的一些二级结构元素是β-转角（其中Pro可与相邻的芳族残基相互作用）和反平行β-折叠（在反平行β-折叠中），其中边缘链中的Pro可与芳族残基相互作用非氢键位点的相邻链。 Calpha和Cdelta位置的CH基团可以形成很强的CH ... O相互作用（从点的聚类中可以看出），这种相互作用涉及C'位置相对于α-螺旋的Pro残基，可以封盖氢键的形成螺旋C末端的游离羰基电位出现在蛋白质结合位点上的功能重要的Pro残基几乎总是与复合物中伴侣分子的芳香残基（其中一个由C-H ... pi相互作用保持）结合，并且此类芳香残基在进化过程中高度保守。

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