Biochemistry on a leash: the roles of tether length and geometry in signal integration proteins.
Biophys J
; 96(4): 1275-92, 2009 Feb 18.
Article
en En
| MEDLINE
| ID: mdl-19217847
We use statistical mechanics and simple ideas from polymer physics to develop a quantitative model of proteins whose activity is controlled by flexibly tethered ligands and receptors. We predict how the properties of tethers influence the function of these proteins and demonstrate how their tether length dependence can be exploited to construct proteins whose integration of multiple signals can be tuned. One case study to which we apply these ideas is that of the Wiskott-Aldrich Syndrome Proteins as activators of actin polymerization. More generally, tethered ligands competing with those free in solution are common phenomena in biology, making this an important specific example of a widespread biological idea.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Conformación Proteica
/
Transducción de Señal
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Familia de Proteínas del Síndrome de Wiskott-Aldrich
/
Modelos Químicos
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Biophys J
Año:
2009
Tipo del documento:
Article
País de afiliación:
Estados Unidos