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Publication : Molecular and serological analysis of polymorphisms in the murine major histocompatibility complex-encoded proteasome subunits, LMP-2 and LMP-7.

First Author  Nandi D Year  1996
Journal  Exp Clin Immunogenet Volume  13
Issue  1 Pages  20-9
PubMed ID  8854085 Mgi Jnum  J:35211
Mgi Id  MGI:82664 Citation  Nandi D, et al. (1996) Molecular and serological analysis of polymorphisms in the murine major histocompatibility complex-encoded proteasome subunits, LMP-2 and LMP-7. Exp Clin Immunogenet 13(1):20-9
abstractText  LMP-2 and LMP-7, gamma-interferon-inducible subunits of the 20S proteasome, play an important role in antigen processing. To define the molecular basis of their polymorphism, we sequenced Lmp-2 and Lmp-7 cDNA from nine different strains of mice. Three allelic variants of both LMP-2 and LMP-7 were found, but all of the polymorphism in LMP-7 is clustered near the carboxyl terminus of the molecule. We confirmed the nucleotide sequence changes at the protein level in both the unprocessed and processed forms of the molecules by analysis of specific anti-LMP-2, anti-LMP-7 and anti-proteasome immunoprecipitates on two- dimensional PAGE gels. Interestingly, a single amino acid change at position 272 between LMP-7(b, d, q) and LMP-7(k, s, f, r, g7, cas4) from glycine to arginine dramatically affects its migration on SDS-PAGE gels, suggesting the possibility of allele-specific posttranslational modification.
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