首页> 美国卫生研究院文献>Arthritis Research >The increased ability to present citrullinated peptides is not unique to HLA-SE molecules: arginine-to-citrulline conversion also enhances peptide affinity for HLA-DQ molecules
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The increased ability to present citrullinated peptides is not unique to HLA-SE molecules: arginine-to-citrulline conversion also enhances peptide affinity for HLA-DQ molecules

机译:呈递瓜氨酸化肽的能力增强并非HLA-SE分子独有:精氨酸向瓜氨酸的转化还增强了对HLA-DQ分子的肽亲和力

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摘要

BackgroundPresentation of citrullinated neo-epitopes by HLA-DRB1 molecules that carry the shared epitope (SE) sequence was proposed to explain the association between HLA and seropositive RA. Although it is shown that several HLA-DRB1-SE molecules display enhanced binding affinities for citrullinated ligands, the ability of other HLA molecules to present citrullinated epitopes has not been investigated in a systematic manner. To better understand the HLA-RA connection, we aimed to investigate if the enhanced capacity to present arginine-to-citrulline-converted peptides is unique for HLA-SE alleles.
机译:背景提出了带有共享表位(SE)序列的HLA-DRB1分子对瓜氨酸化的新表位的表达,以解释HLA与血清阳性RA之间的联系。尽管已显示几种HLA-DRB1-SE分子显示出对瓜氨酸化配体的增强的结合亲和力,但尚未以系统的方式研究其他HLA分子呈递瓜氨酸化表位的能力。为了更好地了解HLA-RA之间的联系,我们旨在研究呈递精氨酸到瓜氨酸转化的肽的增强能力对于HLA-SE等位基因是否独特。

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