Revealing the peptide presenting process of human leukocyte antigen through the analysis of fluctuation.

Biophysics (Nagoya-shi, Japan) Pub Date : 2015-04-18 eCollection Date: 2015-01-01 DOI:10.2142/biophysics.11.103
Saeko Yanaka, Takamasa Ueno, Kouhei Tsumoto, Kenji Sugase
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引用次数: 2

Abstract

Structural fluctuation on microsecond to millisecond time scales has been reported to play an important role in proteins that undergo significant structural change during their expression of function. In these proteins, the structural change was obvious in the crystal structures. However, protein motions in solution could contribute to the function of proteins, even if no significant structural difference is observed in crystal structure of different states while they function. In this review, we introduce our recent report on the stabilization mechanism of human leukocyte antigen, and the possibility of fluctuation contributing to several biophysical properties of proteins.

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通过波动分析揭示人白细胞抗原的肽递呈过程。
据报道,在微秒到毫秒时间尺度上的结构波动在蛋白质的功能表达过程中发生重大的结构变化中起重要作用。在这些蛋白质中,晶体结构发生了明显的结构变化。然而,蛋白质在溶液中的运动可以促进蛋白质的功能,即使不同状态的晶体结构在它们的功能中没有明显的结构差异。在这篇综述中,我们介绍了我们最近对人类白细胞抗原稳定机制的报道,以及波动对蛋白质几种生物物理特性的影响的可能性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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