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Titolo:
TAP association influences the conformation of nascent MHC class I molecules
Autore:
Owen, BAL; Pease, LR;
Indirizzi:
Mayo Clin & Mayo Fdn, Dept Immunol, Rochester, MN 55905 USA Mayo Clin & Mayo Fdn Rochester MN USA 55905 unol, Rochester, MN 55905 USA Mayo Clin & Mayo Fdn, Dept Biochem & Mol Biol, Rochester, MN 55905 USA Mayo Clin & Mayo Fdn Rochester MN USA 55905 Biol, Rochester, MN 55905 USA Mayo Clin & Mayo Fdn, Dept Biochem, Rochester, MN 55905 USA Mayo Clin & Mayo Fdn Rochester MN USA 55905 chem, Rochester, MN 55905 USA Mayo Clin & Mayo Fdn, Dept Biol Mol, Rochester, MN 55905 USA Mayo Clin & Mayo Fdn Rochester MN USA 55905 Mol, Rochester, MN 55905 USA
Titolo Testata:
JOURNAL OF IMMUNOLOGY
fascicolo: 8, volume: 162, anno: 1999,
pagine: 4677 - 4684
SICI:
0022-1767(19990415)162:8<4677:TAITCO>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
MAJOR HISTOCOMPATIBILITY COMPLEX; NEGATIVE CELL-LINE; ENDOPLASMIC-RETICULUM; PEPTIDE TRANSPORTER; MESSENGER-RNA; T-CELLS; ANTIGEN; TAPASIN; DEFICIENT; BINDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Pease, LR MayoMNlin & Mayo Fdn, Dept Immunol, Guggenheim 3,200 1st St SW, Rochester, Mayo Clin & Mayo Fdn Guggenheim 3,200 1st St SW Rochester MN USA55905
Citazione:
B.A.L. Owen e L.R. Pease, "TAP association influences the conformation of nascent MHC class I molecules", J IMMUNOL, 162(8), 1999, pp. 4677-4684

Abstract

The influence of TAP-MHC class I interactions on peptide binding to the class I heavy chain is assessed during TAP-dependent assembly using K-b-specific Abs that recognize conformational changes induced by assembly with beta(2)-microglobulin (beta(2)m) and by peptide binding. A significant portion (45%) of K-b molecules in TAP(+), RMA-derived microsomes are associated with the TAP complex as measured by coimmunoisolation of K-b using anti-TAP1 Abs, while only 20% of the K-b heavy chain molecules are isolated as K(b)beta(2)m complexes with the alpha-K-b-specific Abs, Y-3 or K-10-56. The amountof K-b isolated with Y-3 and K-10-56 increases in proportion to transport and binding of peptide to the K-b molecules within the RMA microsomes. In contrast, less than 5% of the K-b within TAP2-RMA-S microsomes associated with the remaining TAP1 subunit, However, greater than 60% of K-b heavy chainis isolated as K-10-56- and Y-3-reactive K(b)beta(2)m complexes. We propose that a TAP-MHC class I interaction serves to stabilize the MHC class I:beta(2)m complex in an immature conformation (Y-3 and K-10-56 nonreactive) prior to high affinity peptide binding? preventing the export of class I molecules complexed with low affinity peptide ligands from the ER.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 12:50:12