Skip to main content
. 2019 Sep 9;17(9):e3000436. doi: 10.1371/journal.pbio.3000436

Fig 3. Overview of Ptal-N*01:01/peptide structures.

Fig 3

(A) Overview of the structure of the Ptal-N*01:01/HeV1. The peptide HeV1 is presented as yellow sticks in the peptide-binding cleft. The heavy chain of Ptal-N*01:01 and bat β2m are shown as green and cyan cartoons, respectively. (B) The superimposition of different Ptal-N*01:01 complexes was performed using the determined structures: Ptal-N*01:01/HeV1, Ptal-N*01:01/HeV2, Ptal-N*01:01/EBOV-NP1, Ptal-N*01:01/EBOV-NP2, Ptal-N*01:01/H17N10-NP, and Ptal-N*01:01/MERS-CoV-S3. The peptides were omitted. (C) Structural alignment of MHC I heavy chains and β2m exhibited a similar overall conformation of Ptal-N*01:01 (green, peptide HeV1), HLA-A*0201 (yellow, PDB code: 3I6G), and H-2Kd (purple, PDB code: 5GR7). (D) The superimposition of the α1α2 domains of Ptal-N*01:01 (green) with other vertebrate MHC I molecules: human HLA-A*0201 (3I6G), macaque Mamu-A*02 (3JTT), swine SLA-1*0401 (3QQ4), equine Eqca-N*00602 (4ZUU), bovine N*01801 (3PWV), canine DLA-88*50801 (5F1I), and murine H2-Kd (5GR7) (all in white). The distinct conformations at the N terminus between the α1-helices of Ptal-N*01:01 (green) and the MHC I from other vertebrates (white) are labeled by a pink circle. The peptide HeV1 in Ptal-N*01:01 is presented in yellow loops. (E) The structural alignment of Ptal-N*01:01 (peptide HeV1) when renatured with bat β2m (green) and human β2m (yellow). HeV1 showed similar conformation in the binding groove. (F) The black box in the dashed line indicates the similar conformations of residues in the interface of the bat (green) and human β2m (yellow) binding to α1α2 domains of Ptal-N*01:01 heavy chain. (G) Similar binding of Ptal-N*01:01 heavy chain to bat and human β2m. Trp60 in bat β2m (cyan) and human β2m (orange) binds to Gln99 and Asp125 in Ptal-N*01:01 when forming a complex. (H) The alignment of monomer bat β2m (blue) with HeV-1/Ptal-N*01:01-batβ2m (green) complexes. Resides Ser55 to Tyr63 in monomer bat β2m (light blue) shift minorly after forming a complex (cyan). β2m, β2-microglobulin; EBOV, Ebola virus; HeV, Hendra virus; MERS-CoV, Middle East respiratory syndrome coronavirus; MHC, major histocompatibility complex; PDB, Protein Data Bank.