Dynamic influence of the two membrane-proximal immunoglobulin-like domains upon the peptide-binding platform domain in class I and class II major histocompatibility complexes: normal mode analysis.
Chem Pharm Bull (Tokyo)
; 57(11): 1193-9, 2009 Nov.
Article
en En
| MEDLINE
| ID: mdl-19881266
ABSTRACT
Major histocompatibility complexes (MHCs) mainly fall into class I and class II. The two classes have similar structures, with two membrane-proximal immunoglobulin-like domains and a peptide-binding platform domain, though their organizations are different. We simulated the dynamics of a whole and partial model deficient in either of the two membrane-proximal domains for class I and class II using normal mode analysis. Our study showed that the influence of the two membrane-proximal domains upon the dynamics of the platform domain were decisively different between class II and class I. Both membrane-proximal domains (the alpha2 and beta2 domains) of class II MHC, especially the alpha2 domain, influenced the most important pocket that accommodates a large hydrophobic anchor side chain of the N-terminal side of the bound peptide, though the pocket was not in the alpha2 domain neighborhood. By contrast, the two membrane-proximal domains (the alpha3 and beta2m domains) of class I MHC had little influence upon the most important pocket that accommodates the N-terminal residue of the bound peptide. These results suggest that the two membrane-proximal domains of class II MHC have a greater influence upon peptide-binding than those of class I MHC.
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Bases de datos:
MEDLINE
Asunto principal:
Péptidos
/
Simulación por Computador
/
Inmunoglobulinas
/
Antígenos de Histocompatibilidad Clase I
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Antígenos de Histocompatibilidad Clase II
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Simulación de Dinámica Molecular
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Modelos Químicos
Límite:
Humans
Idioma:
En
Revista:
Chem Pharm Bull (Tokyo)
Año:
2009
Tipo del documento:
Article
País de afiliación:
Japón