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6J2E

Crystal structure of bat (Pteropus Alecto) MHC class I Ptal-N*01:01 in complex with Ebola virus-derived peptide EBOV-NP1

Summary for 6J2E
Entry DOI10.2210/pdb6j2e/pdb
DescriptorMHC class I antigen, Beta-2-microglobulin, EBOV-NP1, ... (4 entities in total)
Functional Keywordsimmune system
Biological sourcePteropus alecto (Black flying fox)
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Total number of polymer chains6
Total formula weight90051.17
Authors
Lu, D.,Liu, K.F.,Yue, C.,Lu, Q.,Cheng, H.,Chai, Y.,Qi, J.X.,Gao, G.F.,Liu, W.J. (deposition date: 2019-01-01, release date: 2019-09-18, Last modification date: 2024-11-13)
Primary citationLu, 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: 31498797
DOI: 10.1371/journal.pbio.3000436
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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