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实验性自身免疫性神经炎抗原决定簇的构象

Conformation of an antigenic determinant for experimental autoimmune neuritis.

作者信息

Shin H C, Stuart B, McFarlane E F

机构信息

Protein Engineering Laboratory, Hanhyo Institute of Technology, Kyungki-do, Korea.

出版信息

Biochem Biophys Res Commun. 1996 Jul 5;224(1):5-9. doi: 10.1006/bbrc.1996.0975.

Abstract

The conformation of SP-26, the synthetic peptide (residues 53-78) of myelin P2 protein that causes experimental autoimmune neuritis (EAN) in the peripheral nervous system, has been investigated in D2O using Fourier transform infra-red spectroscopy. Turns were found in 26% of the residues in the peptide, with rest of the residues in random coil (72%). The presence of 26% turns agrees well with the number of residues forming three turns in the antigenic region of the intact protein and the number of turns correlates well with the severity of EAN. Since turns also exist in peptides inducing experimental autoimmune encephalomyelitis, the central nervous system counterpart of EAN, turn structure may be a common structural motif for these closely related autoimmune neurological disorders.

摘要

已使用傅里叶变换红外光谱法在重水中研究了SP - 26(髓鞘P2蛋白的合成肽,残基53 - 78)的构象,该肽会在外周神经系统中引发实验性自身免疫性神经炎(EAN)。发现该肽中26%的残基呈转角结构,其余残基呈无规卷曲(72%)。26%的转角结构与完整蛋白抗原区域中形成三个转角的残基数量相符,且转角数量与EAN的严重程度密切相关。由于在诱发实验性自身免疫性脑脊髓炎(EAN的中枢神经系统对应病症)的肽中也存在转角结构,因此转角结构可能是这些密切相关的自身免疫性神经系统疾病的共同结构基序。

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