2cii
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cii OCA], [http://www.ebi.ac.uk/pdbsum/2cii PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cii RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
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, 1FAPGNYPAL9) to promote its folding in vitro of H-2D(b). We found that H-2D(b) can be stabilized by the pentapeptide 5NYPAL9, 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. | 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, 1FAPGNYPAL9) to promote its folding in vitro of H-2D(b). We found that H-2D(b) can be stabilized by the pentapeptide 5NYPAL9, 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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- | ==Disease== | ||
- | Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109700 109700]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Kojima, M.]] | [[Category: Kojima, M.]] | ||
[[Category: Tormo, J.]] | [[Category: Tormo, J.]] | ||
- | [[Category: GOL]] | ||
[[Category: complex (antigen/peptide)]] | [[Category: complex (antigen/peptide)]] | ||
[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:21:59 2008'' |
Revision as of 23:22, 30 March 2008
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, resolution 2.55Å | |||||||
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Sites: | |||||||
Ligands: | |||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
THE CRYSTAL STRUCTURE OF H-2DB COMPLEXED WITH A PARTIAL PEPTIDE EPITOPE SUGGESTS AN MHC CLASS I ASSEMBLY-INTERMEDIATE
Overview
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, 1FAPGNYPAL9) to promote its folding in vitro of H-2D(b). We found that H-2D(b) can be stabilized by the pentapeptide 5NYPAL9, 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.
About this Structure
2CII is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
Reference
The crystal structure of H-2D(b) complexed with a partial peptide epitope suggests a major histocompatibility complex class I assembly intermediate., Glithero A, Tormo J, Doering K, Kojima M, Jones EY, Elliott T, J Biol Chem. 2006 May 5;281(18):12699-704. Epub 2006 Feb 14. PMID:16478731
Page seeded by OCA on Mon Mar 31 02:21:59 2008
Categories: Homo sapiens | Mus musculus | Protein complex | Doering, K. | Elliott, T. | Glithero, A. | Jones, E Y. | Kojima, M. | Tormo, J. | Complex (antigen/peptide) | Glycoprotein | Immune response | Immunoglobulin domain | Membrane | Mhc class i | Mhc i | Peptide binding | Pyrrolidone carboxylic acid | Sendai virus | Transmembrane