6FRR

Structural and immunological properties of the allergen Art v 3

Summary for 6FRR

• Entry DOI: 10.2210/pdb6frr/pdb
• Descriptor: Non-specific lipid-transfer protein, SULFATE ION (3 entities in total)
• Functional Keywords: art v 3.0201 lipid binding protein, allergen
• Biological source: Artemisia vulgaris (Mugwort)
• Total number of polymer chains: 2
• Total formula weight: 20034.97

Authors

Brandstetter, H.,Soh, W.T.,Magler, I. (deposition date: 2018-02-16, release date: 2019-03-13, Last modification date: 2024-01-17)

Primary citation

Wildner, S.,Griessner, I.,Stemeseder, T.,Regl, C.,Soh, W.T.,Stock, L.G.,Volker, T.,Alessandri, C.,Mari, A.,Huber, C.G.,Stutz, H.,Brandstetter, H.,Gadermaier, G.
Boiling down the cysteine-stabilized LTP fold - loss of structural and immunological integrity of allergenic Art v 3 and Pru p 3 as a consequence of irreversible lanthionine formation.
Mol.Immunol., 116:140-150, 2019

PubMed Abstract: Non-specific lipid transfer proteins (LTPs) are important allergens in fruits, pollen, vegetables, nuts and latex. Due to their compact structure, LTPs are highly resistant to heat treatment. Here, Art v 3 from mugwort pollen and Pru p 3 from peach were used as model allergens to in-depth investigate structural and immunological properties upon thermal treatment at different buffer conditions.

PubMed: 31654938
DOI: 10.1016/j.molimm.2019.10.012

Experimental method

X-RAY DIFFRACTION (1.948 Å)