Nom du corpus

Corpus Systématique Animale

Titre du document

Structural correlates of immunoglobulin diversity

Lien vers le document
Éditeur
Springer (journals)
Langue(s) du document
Anglais
Type de document
Research-article
Nom du fichier dans la ressource
Mammiferes_v2b_01083
Auteur(s)
  • Michael Potter
Affiliation(s)
  • Laboratory of Cell Biology, National Cancer Institute, 20205, Bethesda, MD, USA
Résumé

VL and VH domains, from different species and with widely different primary structures, interact with each other in the same way to create the globular Fv region. Much of the Fv is a highly conserved framework structure that is probably common to most, if not all, mammalian Fv regions. The extensive contoured frontal surface of the Fv is composed of highly variable polypeptide segments (Wu-Kabat complementarity-determining regions). These segments are derived from parts of VL, VH, JH gene products and most of the D gene product. This surface is currently considered to be the most likely location of the antigen-binding sites. The firm immunochemical data based on identification of contacting amino acids supporting this location are still, however, very fragmentary. VL and VH gene products form a large part of the potential antigen-reactive surface. Hence, combinations of different VL and VH gene products are the largest source of structural diversity. The JL and JH gene products have chiefly structural functions in maintaining domain architecture and controlling some interactions between VL and VH domains. The VL-J junction amino acid can provide unique structural properties in the deeper accesses of the potential antigen reaction surface. The VHD-JH junction is more superficial and could be, but has not yet been, directly implicated in antigen binding. The D gene product and the additional ammo acids associated with the (VH-D-JH) rearrangement process do determine a substructural part of the potential antigen reactive surface. The D gene product (a connecting segment between two beta strands) can have many different secondary structures. Functionally, the D region product could interact with VL-CDR-1 amino acids to create a specific contour of the antigen reaction surface. Curiously, primary structural variations in H3 have not yet been directly implicated in antigen binding. Much remains to be learned about the role of VH-D-JH rearrangement in antibody diversity. The major genetic factors in creating structural diversity are the multiple VL and VH gene libraries. The gene rearrangement process provides a further amplification. Somatic mutations are yet another additional mechanism.

Catégories Science-Metrix
  • 1 - health sciences
  • 2 - clinical medicine
  • 3 - immunology
Catégories INIST
  • 1 - sciences appliquees, technologies et medecines
  • 2 - sciences biologiques et medicales
  • 3 - sciences biologiques fondamentales et appliquees. psychologie
Catégories Scopus
  • 1 - Life Sciences ; 2 - Immunology and Microbiology ; 3 - Immunology
Catégories WoS
  • 1 - science ; 2 - immunology
Identifiant ISTEX
AA4C72E2EB56A80242986FEAE0543374050DBEB9
Revue

Survey of Immunologic Research

Année de publication
1983
Présence de XML structuré
Non
Version PDF
1.3
Score qualité du texte
10
Sous-corpus
  • Mammiferes
Type de publication
Journal
ark:/67375/1BB-0T7W9HTT-C
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