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Literature summary for 3.4.22.65 extracted from

  • Chruszcz, M.; Chapman, M.D.; Vailes, L.D.; Stura, E.A.; Saint-Remy, J.M.; Minor, W.; Pomes, A.
    Crystal structures of mite allergens Der f 1 and Der p 1 reveal differences in surface-exposed residues that may influence antibody binding (2009), J. Mol. Biol., 386, 520-530.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Dermatophagoides farinae
-
Dermatophagoides pteronyssinus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+
-
Dermatophagoides pteronyssinus

Organism

Organism UniProt Comment Textmining
Dermatophagoides farinae
-
-
-
Dermatophagoides pteronyssinus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Dermatophagoides farinae
-
Dermatophagoides pteronyssinus

Subunits

Subunits Comment Organism
monomer crystal structure: analysis of the accessible surface area upon dimerization, dimer corresponds most probably to the inactive form Dermatophagoides pteronyssinus
monomer gel filtration, pH 7.5 Dermatophagoides farinae

Synonyms

Synonyms Comment Organism
Der f 1
-
Dermatophagoides farinae
Der p 1
-
Dermatophagoides pteronyssinus