8TI7

Crystal structure of profilin from Dermatophagoides pteronyssinus in complex with a poly(L-proline) peptide

Summary for 8TI7

• Entry DOI: 10.2210/pdb8ti7/pdb
• Descriptor: Profilin, poly(L-proline), SULFATE ION, ... (4 entities in total)
• Functional Keywords: mite profilin, dust mite, allergy, allergen
• Biological source: Dermatophagoides pteronyssinus (European house dust mite); More
• Total number of polymer chains: 16
• Total formula weight: 146211.06

Authors

O'Malley, A.,Sankaran, S.,Chruszcz, M. (deposition date: 2023-07-19, release date: 2024-05-08, Last modification date: 2024-06-19)

Primary citation

O'Malley, A.,Sankaran, S.,Carriuolo, A.,Khatri, K.,Kowal, K.,Chruszcz, M.
Structural homology of mite profilins to plant profilins is not indicative of allergic cross-reactivity.
Biol.Chem., 405:367-381, 2024

PubMed Abstract: Structural and allergenic characterization of mite profilins has not been previously pursued to a similar extent as plant profilins. Here, we describe structures of profilins originating from (registered allergen Tyr p 36.0101) and (here termed Der p profilin), which are the first structures of profilins from Arachnida. Additionally, the thermal stabilities of mite and plant profilins are compared, suggesting that the high number of cysteine residues in mite profilins may play a role in their increased stability. We also examine the cross-reactivity of plant and mite profilins as well as investigate the relevance of these profilins in mite inhalant allergy. Despite their high structural similarity to other profilins, mite profilins have low sequence identity with plant and human profilins. Subsequently, these mite profilins most likely do not display cross-reactivity with plant profilins. At the same time the profilins have highly conserved poly(l-proline) and actin binding sites.

PubMed: 38662449
DOI: 10.1515/hsz-2023-0366

Experimental method

X-RAY DIFFRACTION (2.397 Å)