Protein-protein recognition control by modulating electrostatic interactions.
J Proteome Res
; 9(6): 3118-25, 2010 Jun 04.
Article
em En
| MEDLINE
| ID: mdl-20405930
ABSTRACT
Protein-protein control recognition remains a huge challenge, and its development depends on understanding the chemical and biological mechanisms by which these interactions occur. Here we describe a protein-protein control recognition technique based on the dominant electrostatic interactions occurring between the proteins. We designed a potassium channel inhibitor, BmP05-T, that was 90.32% identical to wild-type BmP05. Negatively charged residues were translocated from the nonbinding interface to the binding interface of BmP05 inhibitor, such that BmP05-T now used BmP05 nonbinding interface as the binding interface. This switch demonstrated that nonbinding interfaces were able to control the orientation of protein binding interfaces in the process of protein-protein recognition. The novel function findings of BmP05-T peptide suggested that the control recognition technique described here had the potential for use in designing and utilizing functional proteins in many biological scenarios.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
/
Engenharia de Proteínas
/
Mapeamento de Interação de Proteínas
/
Domínios e Motivos de Interação entre Proteínas
/
Modelos Biológicos
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
J Proteome Res
Assunto da revista:
BIOQUIMICA
Ano de publicação:
2010
Tipo de documento:
Article