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The Human T-Cell Receptor Repertoire and Transplantation [Paperback]

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  • Category: Books (Medical)
  • ISBN-10:  3662224968
  • ISBN-10:  3662224968
  • ISBN-13:  9783662224960
  • ISBN-13:  9783662224960
  • Publisher:  Springer
  • Publisher:  Springer
  • Pages:  173
  • Pages:  173
  • Binding:  Paperback
  • Binding:  Paperback
  • Pub Date:  01-Mar-2013
  • Pub Date:  01-Mar-2013
  • SKU:  3662224968-11-SPRI
  • SKU:  3662224968-11-SPRI
  • Item ID: 100995581
  • List Price: $109.99
  • Seller: ShopSpell
  • Ships in: 5 business days
  • Transit time: Up to 5 business days
  • Delivery by: Jul 15 to Jul 17
  • Notes: Brand New Book. Order Now.
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.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 lƒ¬
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