The interface between tapasin and MHC class I: identification of amino acid residues in both proteins that influence their interaction |
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Authors: | Turnquist Hĕth R Vargas Shanna E Schenk Erin L McIlhaney Mary M Reber Adrian J Solheim Joyce C |
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Institution: | (1) Eppley Institute for Research in Cancer and Allied Diseases, Department of Pathology and Microbiology, University of Nebraska Medical Center, 986805 Nebraska Medical Center, 68198-6805 Omaha, NE;(2) Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, 986805 Nebraska Medical Center, 68198-6805 Omaha, NE |
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Abstract: | Prior to the binding of antigenic peptide, a complex of chaperone proteins associates with the Major Histocompatibility Complex
(MHC) class I heavy chain/β2m heterodimer. Although each dornain of the MHC class I heavy chain contains amino acid resid uses that influence chaperone
binding, there are several pieces of evidence that point to an interaction between the MHC clas 1α2/α3 domains and tapasin.
In egard to the site on tapasin involved in the tapasin/MHC interface, we have found that a particular region of tapasin (containing
amino acid residues 334–342) is necessary for the binding of tapasin to the MHC class I heavy chain. Our results also indicate
that amino acids in this region of tapasin also affect the proportion of MHC class I open forms expressed at the cell surface
and MHC class I egress from the endoplasmic reticulurn. Based on these results and those obtained by other laboratories, a
model for MHC class I/tapasin interaction is proposed. |
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Keywords: | Antigen presentation Chaperone Major histocompatibility complex class I Tapasin Transporter associated with antigen processing |
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