Structure of the house dust mite allergen Der f 2: Implications for function and molecular basis of IgE cross-reactivityStructure of the house dust mite allergen Der f 2: Implications for function and molecular basis of IgE cross-reactivity

Structural highlights

1xwv is a 2 chain structure with sequence from Dermatophagoides farinae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.83Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ALL2_DERFA

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The X-ray structure of the group 2 major allergen from Dermatophagoides farinae (Der f 2) was determined to 1.83 A resolution. The overall Der f 2 structure comprises a single domain of immunoglobulin fold with two anti-parallel beta-sheets. A large hydrophobic cavity is formed in the interior of Der f 2. Structural comparisons to distantly related proteins suggest a role in lipid binding. Immunoglobulin E (IgE) cross-reactivity between group 2 house dust mite major allergens can be explained by conserved surface areas representing IgE binding epitopes.

Structure of the house dust mite allergen Der f 2: implications for function and molecular basis of IgE cross-reactivity.,Johannessen BR, Skov LK, Kastrup JS, Kristensen O, Bolwig C, Larsen JN, Spangfort M, Lund K, Gajhede M FEBS Lett. 2005 Feb 14;579(5):1208-12. Epub 2005 Jan 21. PMID:15710415[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Johannessen BR, Skov LK, Kastrup JS, Kristensen O, Bolwig C, Larsen JN, Spangfort M, Lund K, Gajhede M. Structure of the house dust mite allergen Der f 2: implications for function and molecular basis of IgE cross-reactivity. FEBS Lett. 2005 Feb 14;579(5):1208-12. Epub 2005 Jan 21. PMID:15710415 doi:10.1016/j.febslet.2004.11.115

1xwv, resolution 1.83Å

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