The crystal structure of H-2D(b) complexed with a partial peptide epitope suggests a major histocompatibility complex class I assembly intermediate
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. Journal of Biological Chemistry, 281, (18), 12699-12704. (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.
|Keywords:||mhc, absence, resolution, in-vitro, time, tapasin, molecules,3-dimensional structure, expression, t-cell recognition, binding, induced conformational change, bound peptide, stability|
Q Science > QR Microbiology
|Divisions:||University Structure - Pre August 2011 > School of Medicine > Cancer Sciences
University Structure - Pre August 2011 > School of Biological Sciences
University Structure - Pre August 2011 > School of Medicine
|Date Deposited:||11 Sep 2008|
|Last Modified:||01 Jun 2011 02:50|
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