Negatively charged residues interacting with the p4 pocket confer binding specificity to DRB1*0401.
Negatively charged residues interacting with the p4 pocket confer binding specificity to DRB1*0401.
复制标题
带负电荷的残基与 p4 口袋相互作用，赋予 DRB1*0401 结合特异性。
DOI：
10.1002/art.1780381207
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发表时间：
1995
影响因子：
--
通讯作者：
Schwartz,BD
中科院分区：
文献类型：
--
作者：
Woulfe,SL;Bono,CP;Zacheis,ML;Kirschmann,DA;Baudino,TA;Swearingen,C;Karr,RW;Schwartz,BD
客观的。鉴定参与选择性肽与 DRB1*0401 结合的关键残基。方法。使用酶联免疫吸附测定和流式细胞术评估肽与天然或定点突变 DR 分子的结合。结果。 DR 和肽残基上的氨基酸取代预计会促进 DR p4 口袋内的相互作用，对结合特异性的影响最大。结论。 DR 分子肽结合库的差异可能与自身免疫性疾病有关。
Objective. To identify critical residues involved in the binding of a selective peptide to DRB1*0401.Methods. The binding of peptides to native or site‐directed mutant DR molecules was evaluated using enzyme‐linked immunosorbent assay and flow cytometry.Results. Amino acid substitutions at DR and peptide residues, which were predicted to contribute to interactions within the DR p4 pocket, had the greatest effects on the specificity of binding.Conclusion. Differences in the peptide‐binding repertoires of DR molecules may contribute to associations with autoimmune diseases.