The peptide binding site of major histocompatibility complex (MHC) class I molecules is natively unfolded when devoid of peptides. Peptide binding stabilizes the structure and slows the dynamics, but peptide-specific and subtype-specific motions influence, and are influenced by, interaction with assembly chaperones, the T cell receptor, and other class I-binding proteins. The molecular mechanisms of cooperation between peptide, class I heavy chain, and beta-2 microglobulin are insufficiently known but are being elucidated by nuclear magnetic resonance and other modern methods. It appears that micropolymorphic clusters of charged amino acids, often hidden in the molecule interior, determine the dynamics and thus chaperone dependence, cellular fate, and disease association of class I.

中文翻译：

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捕蝇草还是三人行？MHC I 类分子的动力学。

当缺乏肽时，主要组织相容性复合物 (MHC) I 类分子的肽结合位点天然展开。肽结合可稳定结构并减慢动力学，但肽特异性和亚型特异性运动会影响并受其与组装伴侣、T 细胞受体和其他 I 类结合蛋白相互作用的影响。肽、I 类重链和β-2 微球蛋白之间合作的分子机制尚不清楚，但正在通过核磁共振和其他现代方法进行阐明。似乎通常隐藏在分子内部的带电氨基酸的微多态簇决定了 I 类的动力学，从而决定了伴侣依赖性、细胞命运和疾病关联。