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The crystal structure of H-2D(b) complexed with a partial peptide epitope suggests a major histocompatibility complex class I assembly intermediate

The crystal structure of H-2D(b) complexed with a partial peptide epitope suggests a major histocompatibility complex class I assembly intermediate
The crystal structure of H-2D(b) complexed with a partial peptide epitope suggests a major histocompatibility complex class I assembly intermediate
In the absence of bound peptide ligands, major histocompatibility complex (MHC) class I molecules are unstable. In an attempt to determine the minimum requirement for peptide-dependent MHC class I stabilization, we have used short synthetic peptides derived from the Sendai virus nucleoprotein epitope ( residues 324-332, (1)FAPGNYPAL(9)) to promote its folding in vitro of H-2D(b). We found that H-2D(b) can be stabilized by the pentapeptide (5)NYPAL(9), which is equivalent to the C-terminal portion of the optimal nonapeptide and includes both the P5 and P9 anchor residues. We have crystallized the complex of the H-2D(b) molecule with the pentamer and determined the structure to show how a quasi-stable MHC class I molecule can be formed by occupancy of a single binding pocket in the peptide-binding groove.
mhc, absence, resolution, in-vitro, time, tapasin, molecules, 3-dimensional structure, expression, t-cell recognition, binding, induced conformational change, bound peptide, stability
0021-9258
12699-12704
Glithero, Ann
e42ef8eb-f738-4ae5-983c-8f523fd5dacc
Tormo, Jose
514b3143-ac5d-4b20-8b0c-0b4c52222471
Doering, Klaus
1f243886-71a5-4297-b5e5-94b3db8df3b3
Kojima, Mayumi
ec005f9f-5035-4db4-a6dd-396ec2ba2be6
Jones, E. Yvonne
6b9004c9-137b-4f43-8a14-c7c83bcaa4be
Elliott, Tim
16670fa8-c2f9-477a-91df-7c9e5b453e0e
Glithero, Ann
e42ef8eb-f738-4ae5-983c-8f523fd5dacc
Tormo, Jose
514b3143-ac5d-4b20-8b0c-0b4c52222471
Doering, Klaus
1f243886-71a5-4297-b5e5-94b3db8df3b3
Kojima, Mayumi
ec005f9f-5035-4db4-a6dd-396ec2ba2be6
Jones, E. Yvonne
6b9004c9-137b-4f43-8a14-c7c83bcaa4be
Elliott, Tim
16670fa8-c2f9-477a-91df-7c9e5b453e0e

Glithero, Ann, Tormo, Jose, Doering, Klaus, Kojima, Mayumi, Jones, E. Yvonne and Elliott, Tim (2006) The crystal structure of H-2D(b) complexed with a partial peptide epitope suggests a major histocompatibility complex class I assembly intermediate. The Journal of Biological Chemistry, 281 (18), 12699-12704. (doi:10.1074/jbc.M511683200).

Record type: Article

Abstract

In the absence of bound peptide ligands, major histocompatibility complex (MHC) class I molecules are unstable. In an attempt to determine the minimum requirement for peptide-dependent MHC class I stabilization, we have used short synthetic peptides derived from the Sendai virus nucleoprotein epitope ( residues 324-332, (1)FAPGNYPAL(9)) to promote its folding in vitro of H-2D(b). We found that H-2D(b) can be stabilized by the pentapeptide (5)NYPAL(9), which is equivalent to the C-terminal portion of the optimal nonapeptide and includes both the P5 and P9 anchor residues. We have crystallized the complex of the H-2D(b) molecule with the pentamer and determined the structure to show how a quasi-stable MHC class I molecule can be formed by occupancy of a single binding pocket in the peptide-binding groove.

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More information

Published date: 5 May 2006
Keywords: mhc, absence, resolution, in-vitro, time, tapasin, molecules, 3-dimensional structure, expression, t-cell recognition, binding, induced conformational change, bound peptide, stability

Identifiers

Local EPrints ID: 26325
URI: http://eprints.soton.ac.uk/id/eprint/26325
ISSN: 0021-9258
PURE UUID: 8ba4f516-3743-4ada-b743-22bd8d22aa0e
ORCID for Tim Elliott: ORCID iD orcid.org/0000-0003-1097-0222

Catalogue record

Date deposited: 07 Apr 2006
Last modified: 10 Dec 2019 01:48

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