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Alteration within a discrete region of the H-2Ld alpha 1 helix upon association with human beta 2 microglobulin.

Authors
  • Smith, M J
  • Basora, T
  • Kieran, J E
  • Nieto, M C
Type
Published Article
Journal
Immunology and cell biology
Publication Date
Apr 01, 1993
Volume
71 ( Pt 2)
Pages
145–149
Identifiers
PMID: 8486398
Source
Medline
License
Unknown

Abstract

The utilization of the beta 2-microglobulin (B2m) exchange assay allowed for the association of H-2Ld with human B2m. Upon association with H-2Ld, human B2m induces structural alterations in H-2Ld that appear dependent upon xenogeneic B2m amino acid sequence variability. In this regard, xenogeneic B2m exchange is used as a tool to induce structural alterations in class I as a means of analysing the structural-functional relationship of B2m/class I association. Incorporating H-2Ld site-directed mutants into the experimental approach provided strong evidence that B2m makes indirect contact with discrete class I specific amino acid positions located in the helical region of the alpha 1 domain.

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