Glithero, Ann, Tormo, Jose, Doering, Klaus, Kojima, Mayumi, Jones, E. Yvonne and Elliott, Tim
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), . (doi:10.1074/jbc.M511683200).
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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.
|Digital Object Identifier (DOI):
||mhc, absence, resolution, in-vitro, time, tapasin, molecules, 3-dimensional structure, expression, t-cell recognition, binding, induced conformational change, bound peptide, stability
|5 May 2006||Published|
||11 Sep 2008
||16 Apr 2017 17:28
|Further Information:||Google Scholar|
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