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Loss of a glycine in the alpha2 domain affects MHC peptide binding but not chaperone binding.

Abstract：

:Prior to the binding of peptide in the endoplasmic reticulum (ER), the major histocompatibility complex (MHC) class I heavy chain associates with an assembly complex that includes the transporter associated with antigen processing (TAP). The proximity of a part of the MHC class I alpha2 domain alpha-helix to areas previously shown to influence assembly complex binding suggests that this region might also be involved in chaperone association. Position 151, found in this part of the alpha2 domain alpha-helix, has a side chain that points up, away from direct contact with peptide, and is occupied by a glycine in all murine MHC class I heavy chains. We found that substitution of this glycine in H-2L(d) with a histidine substantially increased the proportion of peptide-free forms, although TAP binding was not abrogated. Thus, interaction of the heavy chain with peptides, but not with the assembly complex, is influenced by this glycine.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Turnquist HR,Vargas SE,Solheim JC

doi

10.1006/bbrc.2001.6060

subject

Has Abstract

pub_date

2001-12-14 00:00:00

pages

825-31

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(01)96060-7

journal_volume

289

pub_type

杂志文章

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