《Table 1 ANCHOR-based assessments of disorder among MHC class II peptide epitopes》

  提示：宽带有限、当前游客访问压缩模式

本系列图表出处文件名：随高清版一同展现

《High-level intrinsic disorder explains the universality of CLIP binding to diverse MHC class Ⅱ variants》

1. 获取 高清版本忘记账户？点击这里登录

1. 下载图表忘记账户？点击这里登录

To ensure that there was no fundamental difference between primary MHC class II peptide groove binding and the binding of the TcRs to the polymorphic edges of the groove，we generated a comparison of the CLIP intrinsic disorder with the intrinsic disorder rate among 501 MHC class II bindingpeptides obtained from the immune epitope database（www.iedb.org）.Because all of a given peptide epitope and CLIP represent binding sites for another protein，MHC class II，we also employed the ANCHOR algorithm specifically designed to assess potential intrinsic disorder-based protein binding sites.The ANCHOR algorithm determines binding energy favorability for disorder regions if there is an interaction with another protein.Essentially，the disorder determination is more constrained by the requirement of a significant energy trough upon binding.Nevertheless，CLIP remains unusual:339out of 501 epitope peptides were completely ordered，with no amino acids contributing to the disorder，which is not surprising given the expected high level of chemical bond-specificities necessary to maintaintheepitope，allele-specific MHCII binding interaction（Table 1）.This contrasts with the ANCHOR assessment of CLIP disorder，in which 15 of 24 amino acids constitute intrinsically disorderbased binding.