Structural stability studies in adhesion molecules-role of cation-π interactions

被引：7
|
作者：
Sophiya, K. [1 ]
Anbarasu, Anand [1 ]
机构：
[1] VIT Univ, Sch Biosci & Technol, Bioinformat Div, Vellore 632014, Tamil Nadu, India
来源：
PROTOPLASMA | 2011年 / 248卷 / 04期
关键词：
Adhesion molecules; Cation-pi interactions; Secondary structure; Conservation patterns; Stabilization centers; PROTEIN SECONDARY STRUCTURE; DIFFERENT FOLDING TYPES; STABILIZATION CENTERS; NONLOCAL INTERACTIONS; STRUCTURE PREDICTION; AMINO-ACIDS; IDENTIFICATION; DATABASE; RESIDUES; DETERMINES;
D O I：
10.1007/s00709-010-0224-7
中图分类号：
Q94 [植物学];
学科分类号：
071001 ;
摘要：
Cell adhesion molecules are important for their various roles in many cellular events and responses. In the present study, we have analyzed the roles played by cation-pi interactions in the structural stability of adhesion molecules. These interactions are mainly formed by long-range contacts. The occurrence of arginine is higher than lysine to form cation-pi interactions. The secondary structure preferences of interacting residues are independent of amino acid class. Cation-pi interactions might stabilize the interface between the terminus and core in this class of proteins. The results obtained in the present study will be useful in understanding the contribution of cation-pi interactions to the overall stability of adhesion proteins.
引用
收藏
页码：673 / 682
页数：10
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