3H4Z

Crystal Structure of an MBP-Der p 7 fusion protein


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.35 Å
  • R-Value Free: 0.293 
  • R-Value Work: 0.249 
  • R-Value Observed: 0.249 

wwPDB Validation   3D Report Full Report


This is version 2.2 of the entry. See complete history


Literature

The structure of the dust mite allergen Der p 7 reveals similarities to innate immune proteins.

Mueller, G.A.Edwards, L.L.Aloor, J.J.Fessler, M.B.Glesner, J.Pomes, A.Chapman, M.D.London, R.E.Pedersen, L.C.

(2010) J Allergy Clin Immunol 125: 909-917.e4

  • DOI: https://doi.org/10.1016/j.jaci.2009.12.016
  • Primary Citation of Related Structures:  
    3H4Z

  • PubMed Abstract: 

    Sensitization to house dust mite allergens is strongly correlated with asthma. Der p 7 elicits strong IgE antibody and T-cell responses in patients with mite allergy. However, the structure and biological function of this important allergen are unknown. Allergen function might contribute to allergenicity, as shown for the protease activity of group 1 mite allergens and the interaction with the innate immune system by group 2 mite allergens.


  • Organizational Affiliation

    Laboratory of Structural Biology, National Institute of Environmental Health Sciences, Research Triangle Park, NC, USA. mueller3@niehs.nih.gov


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Maltose-binding periplasmic protein fused with Allergen DERP7
A, B, C
568Escherichia coliDermatophagoides pteronyssinus
This entity is chimeric
Mutation(s): 6 
Gene Names: malEDERP7
UniProt
Find proteins for P49273 (Dermatophagoides pteronyssinus)
Explore P49273 
Go to UniProtKB:  P49273
Find proteins for P0AEX9 (Escherichia coli (strain K12))
Explore P0AEX9 
Go to UniProtKB:  P0AEX9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupsP49273P0AEX9
Sequence Annotations
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  • Reference Sequence
Oligosaccharides

Help

Entity ID: 2
MoleculeChains Length2D Diagram Glycosylation3D Interactions
alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose
D, E, F
2N/A
Glycosylation Resources
GlyTouCan:  G07411ON
GlyCosmos:  G07411ON
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
NA
Query on NA

Download Ideal Coordinates CCD File 
G [auth A]SODIUM ION
Na
FKNQFGJONOIPTF-UHFFFAOYSA-N
Biologically Interesting Molecules (External Reference) 1 Unique
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.35 Å
  • R-Value Free: 0.293 
  • R-Value Work: 0.249 
  • R-Value Observed: 0.249 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 193.352α = 90
b = 117.904β = 114.06
c = 92.441γ = 90
Software Package:
Software NamePurpose
StructureStudiodata collection
MOLREPphasing
CNSrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-03-31
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2017-08-02
    Changes: Refinement description, Source and taxonomy
  • Version 2.0: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Atomic model, Data collection, Derived calculations, Structure summary
  • Version 2.1: 2021-10-13
    Changes: Database references, Structure summary
  • Version 2.2: 2023-09-06
    Changes: Data collection, Refinement description