GTP-dependent conformational changes associated with the functional switch between Galpha and cross-linking activities in brain-derived tissue transglutaminase.
J Mol Biol
; 282(4): 713-20, 1998 Oct 02.
Article
en En
| MEDLINE
| ID: mdl-9743620
GTP and Ca2+, two well-known modulators of intracellular signaling pathways, control a structural/functional switch between two vital and mutually exclusive activities, cross-linking and Galpha activity, in the same enzyme. The enzyme, a brain-derived tissue-type transglutaminase (TGase), was recently cloned by us in two forms, one of which (s-TGN) lacks a C-terminal region that is present in the other (l-TGN). Immunoreaction with antibodies directed against a peptide present in the C-terminus of l-TGN but missing in s-TGN suggested that this site, which is located in the C-terminal fourth domain, undergoes conformational changes as a result of interaction between l-TGN and GTP. Site-directed mutagenesis suggested that the third domain is involved in mediating the inhibition of the cross-linking activity. These results were supported by molecular modeling, which further suggested that domains III and IV both participate in conformational changes leading to the functional switch between the Ca2+-dependent cross-linking activity and the Galpha activity.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Encéfalo
/
Transglutaminasas
/
Proteínas de Unión al GTP
/
Reactivos de Enlaces Cruzados
/
GTP Fosfohidrolasas
/
Guanosina Trifosfato
Tipo de estudio:
Prognostic_studies
/
Risk_factors_studies
Límite:
Animals
/
Humans
Idioma:
En
Revista:
J Mol Biol
Año:
1998
Tipo del documento:
Article
País de afiliación:
Israel
Pais de publicación:
Países Bajos