Homology modeling of allergenic cyclophilins: IgE-binding site and structural basis of cross-reactivity

被引:12
|
作者
Roy, D
Ghosh, D
Gupta-Bhattacharya, S
机构
[1] Bose Inst, Bioinform Ctr, Kolkata 700054, India
[2] Bose Inst, Dept Bot, Kolkata 700054, India
关键词
allergen; cyclophillin; cross-reactivity homology modeling; solvent-accessibility; cyclosporin;
D O I
10.1016/S0006-291X(03)01193-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Cross-reactivity among allergens is of considerable scientific as well as clinical interest. Proteins belonging to the allergenic cyclophilin family share a high degree of sequence homology and are cross-reactive. Until date no three-dimensional structural information is available on these proteins and the shared structural features of the epitopes which are the most important determinants of cross-reactivity. Cyclophilins are also known to bind with the immuno-suppressive drug cyclosporin. Comparative molecular modeling of these allergenic cyclophilin proteins of different sources was performed in order to investigate the structural basis of their cross-reactivity. All the proteins studied revealed a similarity in the shape of the cross-reactive epitopes with varying degrees of accessibility. Cyclosporin binding and allergenic properties of these proteins were also found to be structurally related. (C) 2003 Elsevier Inc. All rights reserved.
引用
收藏
页码:422 / 429
页数:8
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