Literature DB >> 1741401

Polymorphism in a second ABC transporter gene located within the class II region of the human major histocompatibility complex.

S H Powis1, I Mockridge, A Kelly, L A Kerr, R Glynne, U Gileadi, S Beck, J Trowsdale.   

Abstract

Recent studies have identified genes within the major histocompatibility complex (MHC) that may play a role in presentation of antigenic peptides to T cells. We have previously described RING4, a gene within the human MHC class II region that has sequence homology with members of the ABC ("ATP-binding cassette") transporter superfamily. We now report the nucleotide sequence of RING11, a second ABC transporter gene located approximately 7 kilobases telomeric to RING4, RING11 is gamma-interferon inducible, a property shared with other genes involved in antigen presentation. Comparison between the amino acid sequences of RING11 and RING4 reveals strong homology. We propose that they form a heterodimer that transports peptides from the cytoplasm into the endoplasmic reticulum. We have identified two RING11 alleles, which differ in the length of their derived protein sequence by 17 amino acids. The more common of these alleles is present in a Caucasoid population at a frequency of 79%.

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Year:  1992        PMID: 1741401      PMCID: PMC48471          DOI: 10.1073/pnas.89.4.1463

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  45 in total

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4.  The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens.

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Review 6.  Binding protein-dependent transport systems.

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9.  Genetic analysis of the membrane insertion and topology of MalF, a cytoplasmic membrane protein of Escherichia coli.

Authors:  S Froshauer; G N Green; D Boyd; K McGovern; J Beckwith
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6.  Polymorphic peptide transporters in MHC class I monomorphic Syrian hamster.

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9.  Recognition of vaccinia virus-encoded major histocompatibility complex class I antigens by virus immune cytotoxic T cells is independent of the polymorphism of the peptide transporters.

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