The complete amino acid sequence of the murine transplantation antigen H-2Db as deduced by molecular cloning

Abstract

A mouse cDNA library derived from the EL4 cell line (b-haplotype) was screened with a probe containing a small part of the H-2Kb coding region. One of the clones isolated, pH203, encodes a protein whose deduced amino acid sequence is identical with the known sequence of H-2Db in 141 of 141 positions available for comparison. The clone, therefore, is believed to code for the H-2Db transplantation antigen. The cDNA insert of pH203 contains the coding region for residues 82 through the carboxy-terminus of H-2Db, and includes 476 nucleotides of the 3'-untranslated sequence. Comparison between the H-2Db cDNA clone and a previously isolated H-2Kb cDNA clone shows homologies of 83% and 91% at the amino acid and nucleotide levels, respectively. Analysis of DNA sequences at the 3'-coding and untranslated regions suggests that the mRNAs of H-2Kb and H-2Db are spliced differently at their 3'-coding ends.