Homology modeling of the cellulose-binding domain of a pollen allergen from rye grass:: structural basis for the cellulose recognition and associated allergenic properties

被引:21
作者
Barre, A [1 ]
Rougé, P [1 ]
机构
[1] CNRS, UMR 5089, Inst Pharmacol & Biol Struct, F-31077 Toulouse 4, France
关键词
grass pollen allergen Lol pI; expansins; cellulose-binding domain; T-cell epitopes;
D O I
10.1016/S0006-291X(02)02091-0
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
A three-dimensional model of the cellulose-binding domain of the rye-grass pollen allergen Lol pI built by homology modeling is proposed as a structural scaffold for expansins and other expansin-related proteins. A groove and an extended strip of aromatic and polar residues presumably account for the cellulose-binding properties of the protein domain. Two of the four predicted T-cell epitopes readily exposed on the surface of the cellulose-binding domain match with previously reported IgE-binding regions. A close structural relationship occurs between the cellulose-binding and allergenic properties. (C) 2002 Elsevier Science (USA). All rights reserved.
引用
收藏
页码:1346 / 1351
页数:6
相关论文
共 42 条
[41]   Crystal structure of a bacterial family-III cellulose-binding domain: A general mechanism for attachment to cellulose [J].
Tormo, J ;
Lamed, R ;
Chirino, AJ ;
Morag, E ;
Bayer, EA ;
Shoham, Y ;
Steitz, TA .
EMBO JOURNAL, 1996, 15 (21) :5739-5751
[42]  
XUN GY, 1995, BIOCHEMISTRY-US, V34, P6993