The interface between tapasin and MHC class I: Identification of amino acid residues in both proteins that influence their interaction

Immunologic Research

Volumn 25, Issue 3, 2002, Pages 261-269

  Turnquist, Hēth R ^a   Vargas, Shanna E ^a   Schenk, Erin L ^a   McIlhaney, Mary M ^a   Reber, Adrian J ^a   Solheim, Joyce C ^a  

^a UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

Author keywords

Antigen presentation; Chaperone; Major histocompatibility complex class I; Tapasin; Transporter associated with antigen processing

Indexed keywords

AMINO ACID; CHAPERONE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; TAPASIN;

AMINO ACID SEQUENCE; ANTIGEN BINDING; BINDING SITE; ENDOPLASMIC RETICULUM; HUMAN; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; REVIEW;

AMINO ACIDS; ANIMALS; ANTIGEN PRESENTATION; ANTIPORTERS; B-LYMPHOCYTES; CELL LINE; HISTOCOMPATIBILITY ANTIGENS CLASS I; HUMANS; IMMUNOGLOBULINS; MEMBRANE TRANSPORT PROTEINS; MICE; MOLECULAR CHAPERONES;

EID: 0036235698     PISSN: 0257277X     EISSN: None     Source Type: Journal    
DOI: 10.1385/IR:25:3:261     Document Type: Review

References (45)

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3. Roles for calreticulin and a novel glycoprorein, tapasin, in the interaction of MHC class I molecules with TAP
4. 2-microglobulin, class I heavy chain conformation, and tapasin in the interactions of class I heavy chain with calreticulin and the transporter associated with antigen processing
5. 2-microglobulin complexes associate with TAP transporters before peptide binding
6. Interaction of MHC class I molecules with the transporter associated with antigen processing
7. TAP associates with a unique class I conformation, whereas calnexin associates with multiple class I forms in mouse and man
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9. Dependence of peptide binding by MHC class I molecules on their interaction with TAP
10. Elucidation of the genetic basis of the antigen presentation defects in the mutant cell line .220 reveals polymorphism and alternative splicing of the tapasin gene
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26. Point mutations in the α2 domain of HLA-A2.1 define a functionally relevant interaction with TAP
27. Physical and functional association of the major histocompatibility complex class I heavy chain α3 domain with the transporter associated with antigen processing
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