Chaperonin function depends on structure and disorder in co-chaperonin mobile loops.
Pac Symp Biocomput
; : 520-31, 1999.
Article
em En
| MEDLINE
| ID: mdl-10380224
ABSTRACT
Co-chaperonins from diverse organisms exhibit mobile loops which fold into a beta hairpin conformation upon binding to the chaperonin. GroES, Gp31, and human Hsp10 mobile loops exhibit a preference for the beta hairpin conformation in the free co-chaperonins, and the conformational dynamics of the human Hsp10 mobile loop appear to be restricted by nascent hairpin formation. Backbone conformational entropy must weigh against binding of co-chaperonins to chaperonins, and thus the conformational preferences of the loops may strongly influence chaperonin-binding affinity. Indeed, subtle mutations in the loops change GroEL-binding affinity and cause defects in chaperonin function, and these defects can be suppressed by mutations in GroEL which compensate for the changes in affinity. The fact that high-affinity co-chaperonin binding impairs chaperonin function has implications for the mechanism of chaperonin-assisted protein folding.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Chaperoninas
Limite:
Humans
Idioma:
En
Revista:
Pac Symp Biocomput
Assunto da revista:
BIOTECNOLOGIA
/
INFORMATICA MEDICA
Ano de publicação:
1999
Tipo de documento:
Article
País de afiliação:
Estados Unidos
País de publicação:
EEUU
/
ESTADOS UNIDOS
/
ESTADOS UNIDOS DA AMERICA
/
EUA
/
UNITED STATES
/
UNITED STATES OF AMERICA
/
US
/
USA