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Structure paper

TitleCrystal structures of mite allergens Der f 1 and Der p 1 reveal differences in surface-exposed residues that may influence antibody binding.
Journal, issue, pagesJ. Mol. Biol., Vol. 386, Page 520-530, Year 2009
Publish dateNov 4, 2008 (structure data deposition date)
AuthorsChruszcz, M. / Chapman, M.D. / Vailes, L.D. / Stura, E.A. / Saint-Remy, J.M. / Minor, W. / Pomes, A.
External linksJ. Mol. Biol. / PubMed:19136006
MethodsX-ray diffraction
Resolution1.36 - 2 Å
Structure data

PDB-3f5v:
C2 Crystal form of mite allergen DER P 1
Method: X-RAY DIFFRACTION / Resolution: 1.36 Å

PDB-5vpk:
CRYSTAL STRUCTURE OF MITE ALLERGEN DER F 1
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-P6G:
HEXAETHYLENE GLYCOL / precipitant*YM

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • dermatophagoides pteronyssinus (European house dust mite)
  • dermatophagoides farinae (American house dust mite)
KeywordsHYDROLASE / ALLERGY / ASTHMA / DUST MITES / ALLERGEN / GLYCOPROTEIN / PROTEASE / SECRETED / THIOL PROTEASE / ZYMOGEN

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