2VZN

Crystal structure of the major allergen from fire ant venom, Sol i 3

Summary for 2VZN

• Entry DOI: 10.2210/pdb2vzn/pdb
• Descriptor: VENOM ALLERGEN 3 (1 entity in total)
• Functional Keywords: major fire ant allergen, sol i 3, secreted, allergen, cross-reactivity
• Biological source: SOLENOPSIS INVICTA (RED FIRE ANT)
• Total number of polymer chains: 2
• Total formula weight: 49654.16

Authors

Padavattan, S.,Markovic-Housley, Z. (deposition date: 2008-08-05, release date: 2008-09-09, Last modification date: 2023-12-13)

Primary citation

Padavattan, S.,Schmidt, M.,Hoffman, D.R.,Markovic-Housley, Z.
Crystal Structure of the Major Allergen from Fire Ant Venom, Sol I 3
J.Mol.Biol., 383:178-, 2008

PubMed Abstract: Fire ant venom is an extremely potent allergy-inducing agent containing four major allergens, Sol i 1 to Sol i 4, which are the most frequent cause of hypersensitivity reactions to hymenoptera in the southern USA. The crystal structure of recombinant (Baculovirus) major fire ant allergen Sol i 3 has been determined to a resolution of 3.1 A by the method of molecular replacement. The secondary-structure elements of Sol i 3 are arranged in an alpha-beta-alpha sandwich fold consisting of a central antiparallel beta-sheet surrounded on both sides by alpha helices. The overall structure is very similar to that of the homologous wasp venom allergen Ves v 5 with major differences occurring in the solvent-exposed loop regions that contain amino acid insertions. Consequently, the limited conservation of surface chemical properties and topology between Sol i 3 and Ves v 5 may explain the observed lack of relevant cross-reactivity. It is concluded that Sol i 3 recognizes immunoglobulin E antibodies with a distinct set of its own epitopes, which are different from those of Ves v 5. Indeed, the molecular area in Sol i 3 covered by non-conserved residues is large enough to accommodate four unique Sol i 3 epitopes.

PubMed: 18761353
DOI: 10.1016/J.JMB.2008.08.023

Experimental method

X-RAY DIFFRACTION (3.05 Å)