Two conformations of pHLA-A*2402: a supplement to Wolynes' theory / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 1370-1377, 2012.
Article
Dans Chinois
| WPRIM
| ID: wpr-342389
ABSTRACT
Wolynes argued that the track of a protein's folding was directed by the tendency of lowering its energy, and thus when a local minimum of its energy was reached, a relatively stable conformation was formed. However not all of the local minimums will lead the protein to a biologically useful conformation, for those otherwise are called energy traps. Wolynes energy landscape theory and natural selection have well explained the high efficiency of protein folding in vivo, instead of being stuck in energy traps. As to whether a protein can assume different conformations with the same bioactivity, there is no clear answer yet. In this paper, two conformational states of a pHLA-A*2402 are discovered after refolding, and by studying their interactions with TCR and CD8alphaalpha, two conformations of pHLA-A*2402 are confirmed of having escaped from natural selection.
Texte intégral:
Disponible
Indice:
WPRIM (Pacifique occidental)
Sujet Principal:
Conformation des protéines
/
Récepteurs aux antigènes des cellules T
/
Chimie
/
Antigènes CD8
/
Pliage des protéines
/
Métabolisme énergétique
/
Antigène HLA-A24
Limites du sujet:
Humains
langue:
Chinois
Texte intégral:
Chinese Journal of Biotechnology
Année:
2012
Type:
Article
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