PROTEIN-PEPTIDE INTERACTIONS

被引：158
|
作者：
STANFIELD, RL
WILSON, IA
机构：
来源：
CURRENT OPINION IN STRUCTURAL BIOLOGY | 1995年 / 5卷 / 01期
关键词：
D O I：
10.1016/0959-440X(95)80015-S
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：
Proteins can interact with short peptide sequences in a variety of ways that can be sequence dependent or independent, The bound peptides are frequently in an extended conformation but may also adopt beta-turns or alpha-helices as motifs for recognition. The peptides can be completely buried in cavities, bound in grooves or pockets, or form beta-strand type interactions at the protein surface. These various recognition motifs are illustrated by peptide interactions with antibodies, calmodulin, OppA periplasmic binding protein, PapD chaperone, MHC class I and class II molecules, and Src homology (SH) domains 2 and 3.
引用
收藏
页码：103 / 113
页数：11
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