Formation of a Major Histocompatibility Complex Class I Tapasin Disulfide Indicates a Change in Spatial Organization of the Peptide-loading Complex during Assembly-Reference-Cited by-同舟云学术

Formation of a Major Histocompatibility Complex Class I Tapasin Disulfide Indicates a Change in Spatial Organization of the Peptide-loading Complex during Assembly

Published:2008-01 Issue:4 Volume:283 Page:1862-1869
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Chambers Joseph E.,Jessop Catherine E.,Bulleid Neil J.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference28 articles.

1. Evidence for successive peptide binding and quality control stages during MHC class I assembly

2. The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex

3. A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules

4. ER60/ERp57 forms disulfide‐bonded intermediates with MHC class I heavy chain

5. Redox Regulation Facilitates Optimal Peptide Selection by MHC Class I during Antigen Processing

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