6K7U

Crystal structure of beta-2 microglobulin (beta2m) of Bat (Pteropus Alecto)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.202 
  • R-Value Work: 0.195 
  • R-Value Observed: 0.196 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Peptide presentation by bat MHC class I provides new insight into the antiviral immunity of bats.

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.

(2019) PLoS Biol 17: e3000436-e3000436

  • DOI: https://doi.org/10.1371/journal.pbio.3000436
  • Primary Citation of Related Structures:  
    6J2D, 6J2E, 6J2F, 6J2G, 6J2H, 6J2I, 6J2J, 6K7T, 6K7U

  • 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.


  • Organizational Affiliation

    NHC Key Laboratory of Medical Virology and Viral Diseases, National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Beijing, China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Bat beta-2-microglobulinA [auth B]99Pteropus alectoMutation(s): 0 
UniProt
Find proteins for L5K3Y9 (Pteropus alecto)
Explore L5K3Y9 
Go to UniProtKB:  L5K3Y9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupL5K3Y9
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.202 
  • R-Value Work: 0.195 
  • R-Value Observed: 0.196 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 33.707α = 90
b = 114.641β = 90
c = 57.307γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling
CNSphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2019-09-18
    Type: Initial release
  • Version 1.1: 2019-09-25
    Changes: Data collection, Structure summary
  • Version 1.2: 2019-12-04
    Changes: Structure summary