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Signal Sequences Distinguish Class II Histocompatibility Antigen ß Chains of Different Loci
Author(s) -
GUSTAFSSON K.,
WIMAN K.,
LARHAMMAR D.,
RASK L.,
PETERSON P. A.
Publication year - 1984
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1984.tb00904.x
Subject(s) - signal peptide , complementary dna , genetics , biology , peptide sequence , histocompatibility , beta (programming language) , nucleic acid sequence , homology (biology) , human leukocyte antigen , alpha chain , major histocompatibility complex , chain (unit) , microbiology and biotechnology , cd74 , amino acid , gene , antigen , mhc class i , physics , computer science , astronomy , programming language
The signal sequences of two HLA‐DR ß chains and the DR α chain were determined. In addition, the major part of a DC ß‐chain signal sequence was also elucidated. The data were obtained by combining amino acid sequenceanalyses of isolated α and ß chains with nucleotide sequencing of four c DNA clones. All signal sequences comprise 25 amino acids or more. The two HLA‐DR ß‐chain signal sequences are identical and exhibit only marginal homology to the DC ß‐chain signal sequence. No homology is apparent between α‐ and ß‐chain signal sequences. The differences in the signalsequences of the DR and DC ß chains suggest that these sequences may be used to assign ß chains to different loci of the human major histocompatibility complex.

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