6J2F
Crystal structure of bat (Pteropus Alecto) MHC class I Ptal-N*01:01 in complex with Hendra virus-derived peptide HeV2
6J2F の概要
エントリーDOI | 10.2210/pdb6j2f/pdb |
分子名称 | Ptal-N*01:01, beta-2 microglobulin, HeV2, ... (4 entities in total) |
機能のキーワード | immune system |
由来する生物種 | Pteropus alecto (Black flying fox) 詳細 |
タンパク質・核酸の鎖数 | 6 |
化学式量合計 | 89284.47 |
構造登録者 | |
主引用文献 | Lu, D.,Liu, K.,Zhang, D.,Yue, C.,Lu, Q.,Cheng, H.,Wang, L.,Chai, Y.,Qi, J.,Wang, L.F.,Gao, G.F.,Liu, W.J. Peptide presentation by bat MHC class I provides new insight into the antiviral immunity of bats. Plos Biol., 17:e3000436-e3000436, 2019 Cited by PubMed Abstract: Bats harbor many zoonotic viruses, including highly pathogenic viruses of humans and other mammals, but they are typically asymptomatic in bats. To further understand the antiviral immunity of bats, we screened and identified a series of bat major histocompatibility complex (MHC) I Ptal-N*01:01-binding peptides derived from four different bat-borne viruses, i.e., Hendra virus (HeV), Ebola virus (EBOV), Middle East respiratory syndrome coronavirus (MERS-CoV), and H17N10 influenza-like virus. The structures of Ptal-N*01:01 display unusual peptide presentation features in that the bat-specific 3-amino acid (aa) insertion enables the tight "surface anchoring" of the P1-Asp in pocket A of bat MHC I. As the classical primary anchoring positions, the B and F pockets of Ptal-N*01:01 also show unconventional conformations, which contribute to unusual peptide motifs and distinct peptide presentation. Notably, the features of bat MHC I may be shared by MHC I from various marsupials. Our study sheds light on bat adaptive immunity and may benefit future vaccine development against bat-borne viruses of high impact on humans. PubMed: 31498797DOI: 10.1371/journal.pbio.3000436 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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