Peptides in proteins

被引:3
|
作者
Weber, Benedikt [1 ]
Maier, Andreas [1 ]
Buchner, Johannes [1 ]
机构
[1] Tech Univ Munich, Ctr Integrated Prot Sci Munich, Dept Chem, Garching, Germany
关键词
peptides; proteins; IgM; tailpiece; Hsp90; C-terminal extensions; TPR; co-chaperone; INTRINSICALLY DISORDERED PROTEINS; MU HEAVY-CHAIN; ENDOPLASMIC-RETICULUM; IMMUNOGLOBULIN-A; ATPASE ACTIVITY; R2TP COMPLEX; HSP90; IGM; REVEALS; SECRETION;
D O I
10.1002/psc.3235
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
The protein universe as we know is composed of folded structures and intrinsic disordered regions. The latter may adopt structures upon interaction with binding partners. In addition, some proteins contain C-terminal extensions which act as independent functional units in the context of the protein. Since their activity does not depend on the protein context they can be considered as peptides in proteins. To illustrate this principle, we here discuss the C-terminal extensions of IgM antibodies which dictate their assembly and the molecular chaperones Hsp90, Hsp70, and Hsp104 which use C-terminal peptide extensions as a docking site for interaction with different co-chaperones.
引用
收藏
页数:11
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