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Structure paper

TitleStructural homology of mite profilins to plant profilins is not indicative of allergic cross-reactivity.
Journal, issue, pagesBiol. Chem., Vol. 405, Page 367-381, Year 2024
Publish dateJul 19, 2023 (structure data deposition date)
AuthorsO'Malley, A. / Sankaran, S. / Carriuolo, A. / Khatri, K. / Kowal, K. / Chruszcz, M.
External linksBiol. Chem. / PubMed:38662449
MethodsX-ray diffraction
Resolution1.15 - 2.397 Å
Structure data

PDB-8ti5:
Crystal structure of Tyr p 36.0101
Method: X-RAY DIFFRACTION / Resolution: 1.15 Å

PDB-8ti6:
Crystal structure of Tyr p 36.0101
Method: X-RAY DIFFRACTION / Resolution: 1.42 Å

PDB-8ti7:
Crystal structure of profilin from Dermatophagoides pteronyssinus in complex with a poly(L-proline) peptide
Method: X-RAY DIFFRACTION / Resolution: 2.397 Å

PDB-8v5y:
Crystal structure of Tyr p 36.0101 in complex with a poly(L-proline) peptide
Method: X-RAY DIFFRACTION / Resolution: 2.059 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • tyrophagus putrescentiae (arthropod)
  • synthetic construct (others)
  • dermatophagoides pteronyssinus (European house dust mite)
KeywordsALLERGEN / mite profilin / storage mite / allergy / dust mite / poly(L-proline) peptide

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