Homology modeling and characterization of IgE binding epitopes of mountain cedar allergen Jun a 3.

Abstract:

:The Jun a 3 protein from mountain cedar (Juniperus ashei) pollen, a member of group 5 of the family of plant pathogenesis-related proteins (PR-proteins), reacts with serum IgE from patients with cedar hypersensitivity. We used the crystal structures of two other proteins of this group, thaumatin and an antifungal protein from tobacco, both approximately 50% identical in sequence to Jun a 3, as templates to build homology models for the allergen. The in-house programs EXDIS and FANTOM were used to extract distance and dihedral angle constraints from the Protein Data Bank files and determine energy-minimized structures. The mean backbone deviations for the energy-refined model structures from either of the templates is <1 A, their conformational energies are low, and their stereochemical properties (determined with PROCHECK) are acceptable. The circular dichroism spectrum of Jun a 3 is consistent with the postulated beta-sheet core. Tryptic fragments of Jun a 3 that reacted with IgE from allergic patients all mapped to one helical/loop surface of the models. The Jun a 3 models have features common to aerosol allergens from completely different protein families, suggesting that tertiary structural elements may mediate the triggering of an allergic response.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Soman KV,Midoro-Horiuti T,Ferreon JC,Goldblum RM,Brooks EG,Kurosky A,Braun W,Schein CH

doi

10.1016/S0006-3495(00)76410-1

subject

Has Abstract

pub_date

2000-09-01 00:00:00

pages

1601-9

issue

3

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(00)76410-1

journal_volume

79

pub_type

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