How does TAP associate with MHC class I molecules?
- 31 August 1997
- journal article
- review article
- Published by Elsevier BV in Immunology Today
- Vol. 18 (8), 375-379
- https://doi.org/10.1016/s0167-5699(97)01097-9
Abstract
No abstract availableThis publication has 12 references indexed in Scilit:
- Roles for Calreticulin and a Novel Glycoprotein, Tapasin, in the Interaction of MHC Class I Molecules with TAPImmunity, 1996
- MHC class I molecules form ternary complexes with calnexin and TAP and undergo peptide-regulated interaction with TAP via their extracellular domains.The Journal of Experimental Medicine, 1996
- Point mutations in the α2 domain of HLA-A2.1 define a functionally relevant interaction with TAPCurrent Biology, 1996
- An Altered Position of the α2 Helix of MHC Class I Is Revealed by the Crystal Structure of HLA-B*3501Immunity, 1996
- Dependence of Peptide Binding by MHC Class I Molecules on Their Interaction with TAPScience, 1995
- The Three-Dimensional Structure of Peptide-MHC ComplexesAnnual Review of Immunology, 1995
- Analysis of the structure of empty and peptide-loaded major histocompatibility complex molecules at the cell surface.The Journal of Experimental Medicine, 1994
- MHC class l/β2-microglobulin complexes associate with TAP transporters before peptide bindingNature, 1994
- Peptide selection by class I molecules of the major histocompatibility complexCurrent Biology, 1993
- Peptide-induced conformational change of the class I heavy chainNature, 1991