The function of the ?3 interactive domain in the small heat shock protein and molecular chaperone, human ?B crystallin
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The function of the ?3 interactive domain in the small heat shock protein and molecular chaperone, human ?B crystallin
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| Id. |
16279563 |
| Idioma |
inglés
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| Titulo |
The function of the ?3 interactive domain in the small heat shock protein and molecular chaperone, human ?B crystallin |
| Autor(es) |
Ghosh, Joy G.
Estrada, Marcus R.
Houck, Scott A.
Clark, John I.
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| Localización |
http://www.pubmedcentral.gov/articlerender.fcgi?artid=1484519
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| Versión |
1.0 |
| Estado |
Final
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| Descripción |
Knowledge of the interactive domains on the surface of small heat shock proteins (sHSPs) is necessary for understanding the assembly of complexes and the activity as molecular chaperones. The primary sequences of 26 sHSP molecular chaperones were aligned and compared. In the interactive ?3 sequence, 73DRFSVNLDVKHFS85 of human ?B crystallin, Ser-76, Asn-78, Lys-82, and His-83 were identified as nonconserved residues on the exposed surface of the ? crystallin core domain. Site-directed mutagenesis produced the mutant ?B crystallins: S76E, N78G, K82Q, and H83F. Domain swapping with homologous ?3 sequences, 32EKFEVGLDVQFFT44 from Caenorhabditis elegans sHSP12.2 or 69DKFVIFLDVKHFS81 from ?A crystallin, resulted in the mutant ?B crystallins, CE1 and ?A1, respectively. Decreased chaperone activity was observed with the point mutants N78G, K82Q, and H83F and with the mutant, CE1, in aggregation assays using ?L crystallin, alcohol dehydrogenase (ADH), or citrate synthase (CS). The S76E mutant had minimal effect on chaperone activity, and domain swapping with ?A crystallin had no effect on chaperone activity. The mutations that resulted in altered chaperone activity, produced minimal modification to the secondary, tertiary, and quaternary structure of human ?B crystallin as determined by ultraviolet circular dichroism spectroscopy, chymotrypsin proteolysis, and size exclusion chromatography. Chaperone activity was influenced by the amount of unfolding of the target proteins and independent of complex size. The results characterized the importance of the exposed side chains of Glu-78, Lys-82, and His-83 in the interactive ?3 sequence of the ? crystallin core domain in ?B crystallin for chaperone function.
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| Palabras clave |
Original Articles
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| Tipo de recurso |
Text
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| Tipo de Interactividad |
Expositivo
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| Nivel de Interactividad |
muy bajo
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| Audiencia |
Estudiante
Profesor
Autor
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| Estructura |
Atomic |
| Coste |
no
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| Copyright |
sí
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Copyright © 2006, Cell Stress Society International |
| Requerimientos técnicos |
Browser: Any
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| Fecha de contribución |
02-dic-2006 |
| Contacto |
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