Unique biochemical properties of a mutant MHC class I molecule, H-2Ksm1.

Abstract:

:This study describes serological and biochemical properties of a novel MHC class I molecule. The mutant H-2Ksm1 molecule was discovered in a mouse because of loss of reactivity of its peripheral blood lymphocytes to monoclonal antibodies. This mutation in the H-2Ks molecule is the first in vivo mutation described that has altered an amino acid residue (amino acid 107) distant from the regions generally considered to be peptide or TCR contacts. Cell surface expression of the mutant molecules remains high but the Arg107 to Trp substitution appears to alter the native protein conformation, markedly decreasing cell surface association with beta 2-microglobulin light chains and conferring a loss of recognition by Ks specific antibodies.

journal_name

Mol Immunol

journal_title

Molecular immunology

authors

Hasenkrug KJ,Kesari KV,Nathenson SG

doi

10.1016/0161-5890(92)90223-k

subject

Has Abstract

pub_date

1992-12-01 00:00:00

pages

1493-500

issue

12

eissn

0161-5890

issn

1872-9142

journal_volume

29

pub_type

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