8ti7

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

spinqualitylabelsall models 8ti7, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8ti7 is a 16 chain structure with sequence from Dermatophagoides pteronyssinus and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.397Å Ligands: SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A2L0EBJ5_DERPT Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations.[RuleBase:RU003908] Publication Abstract from PubMed 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 Tyrophagus putrescentiae (registered allergen Tyr p 36.0101) and Dermatophagoides pteronyssinus (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. Structural homology of mite profilins to plant profilins is not indicative of allergic cross-reactivity.,O'Malley A, Sankaran S, Carriuolo A, Khatri K, Kowal K, Chruszcz M Biol Chem. 2024 Apr 26. doi: 10.1515/hsz-2023-0366. PMID:38662449 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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