Articles liés à The Human T-Cell Receptor Repertoire and Transplantation

The Human T-Cell Receptor Repertoire and Transplantation - Couverture souple

 
9783662224960: The Human T-Cell Receptor Repertoire and Transplantation
Couverture souple
ISBN 10 : 3662224968 ISBN 13 : 9783662224960
Editeur : Springer, 2013

Synopsis

these analyses it became clear that the MHC class I molecule com­ prised a distinct groove on the external side of the molecule. The sides of the groove are formed by the a-helical structures of the a and a 1 2 domains and a floor which is formed by 8 anti-parallel 13 strands. The various polymorphic residues, as determined from DNA sequence analysis, are localized within these a-helices and 13-plated sheets within the groove. More importantly, these analyses also revealed the presence of elec­ tron-dense material in the groove. This material was subsequently iden­ 568 10 tified as a linear peptide of 8-10 amino acids long. - High resolu­ tion crystallographic analyses of the class I MHC structure have revealed the existence of so-called pockets within the grooves of the MHC class I molecules. These pockets designated A-F, exhibited allele-specificity and are directly involved in the binding of the peptide, primarily through interaction with the dominant anchor residues as found in MHC class I associated pep tides. 6,7,9,11 The class II MHC antigens consist on the cell surface of a 34 kD a chain non-covalently associated with a 28 kD 13 chain. With the excep­ tion of the DR a-chain, all other MHC class II a and 13 chains are poly­ morphic.

Les informations fournies dans la section « Synopsis » peuvent faire référence à une autre édition de ce titre.

À propos de la quatrième de couverture

these analyses it became clear that the MHC class I molecule com­ prised a distinct groove on the external side of the molecule. The sides of the groove are formed by the a-helical structures of the a and a 1 2 domains and a floor which is formed by 8 anti-parallel 13 strands. The various polymorphic residues, as determined from DNA sequence analysis, are localized within these a-helices and 13-plated sheets within the groove. More importantly, these analyses also revealed the presence of elec­ tron-dense material in the groove. This material was subsequently iden­ 568 10 tified as a linear peptide of 8-10 amino acids long. ¿ ¿- High resolu­ tion crystallographic analyses of the class I MHC structure have revealed the existence of so-called pockets within the grooves of the MHC class I molecules. These pockets designated A-F, exhibited allele-specificity and are directly involved in the binding of the peptide, primarily through interaction with the dominant anchor residues as found in MHC class I associated pep tides. 6,7,9,11 The class II MHC antigens consist on the cell surface of a 34 kD a chain non-covalently associated with a 28 kD 13 chain. With the excep­ tion of the DR a-chain, all other MHC class II a and 13 chains are poly­ morphic.

Les informations fournies dans la section « A propos du livre » peuvent faire référence à une autre édition de ce titre.

Éditeur
Springer
Date d'édition
2013
Langue
anglais
ISBN 10 
3662224968
ISBN 13 
9783662224960
Reliure
Broché
Nombre de pages
184
Éditeur
Elsen Peter Van Den
Coordonnées du fabricant
ProductSafety@springernature.com
ProductSafety@springernature.com

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