2esv

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|PDB= 2esv |SIZE=350|CAPTION= <scene name='initialview01'>2esv</scene>, resolution 2.600&Aring;
|PDB= 2esv |SIZE=350|CAPTION= <scene name='initialview01'>2esv</scene>, resolution 2.600&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=IOD:IODIDE ION'>IOD</scene>
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|LIGAND= <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2esv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2esv OCA], [http://www.ebi.ac.uk/pdbsum/2esv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2esv RCSB]</span>
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==Overview==
==Overview==
In contrast to antigen-specific immunity orchestrated by major histocompatibility complex (MHC) class Ia molecules, the ancestrally related nonclassical MHC class Ib molecules generally mediate innate immune responses. Here we have demonstrated the structural basis by which the MHC class Ib molecule HLA-E mediates an adaptive MHC-restricted cytotoxic T lymphocyte response to human cytomegalovirus. Highly constrained by host genetics, the response showed notable fine specificity for position 8 of the viral peptide, which is the sole discriminator of self versus nonself. Despite the evolutionary divergence of MHC class Ia and class Ib molecules, the structure of the T cell receptor-MHC class Ib complex was very similar to that of conventional T cell receptor-MHC class Ia complexes. These results emphasize the evolutionary 'ambiguity' of HLA-E, which not only interacts with innate immune receptors but also has the functional capacity to mediate virus-specific cytotoxic T lymphocyte responses during adaptive immunity.
In contrast to antigen-specific immunity orchestrated by major histocompatibility complex (MHC) class Ia molecules, the ancestrally related nonclassical MHC class Ib molecules generally mediate innate immune responses. Here we have demonstrated the structural basis by which the MHC class Ib molecule HLA-E mediates an adaptive MHC-restricted cytotoxic T lymphocyte response to human cytomegalovirus. Highly constrained by host genetics, the response showed notable fine specificity for position 8 of the viral peptide, which is the sole discriminator of self versus nonself. Despite the evolutionary divergence of MHC class Ia and class Ib molecules, the structure of the T cell receptor-MHC class Ib complex was very similar to that of conventional T cell receptor-MHC class Ia complexes. These results emphasize the evolutionary 'ambiguity' of HLA-E, which not only interacts with innate immune receptors but also has the functional capacity to mediate virus-specific cytotoxic T lymphocyte responses during adaptive immunity.
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==Disease==
 
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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: Hoare, H L.]]
[[Category: Hoare, H L.]]
[[Category: Rossjohn, J.]]
[[Category: Rossjohn, J.]]
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[[Category: IOD]]
 
[[Category: cmv]]
[[Category: cmv]]
[[Category: hla-e]]
[[Category: hla-e]]
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[[Category: tcr]]
[[Category: tcr]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:44:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:53:25 2008''

Revision as of 23:53, 30 March 2008


PDB ID 2esv

Drag the structure with the mouse to rotate
, resolution 2.600Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Structure of the HLA-E-VMAPRTLIL/KK50.4 TCR complex


Overview

In contrast to antigen-specific immunity orchestrated by major histocompatibility complex (MHC) class Ia molecules, the ancestrally related nonclassical MHC class Ib molecules generally mediate innate immune responses. Here we have demonstrated the structural basis by which the MHC class Ib molecule HLA-E mediates an adaptive MHC-restricted cytotoxic T lymphocyte response to human cytomegalovirus. Highly constrained by host genetics, the response showed notable fine specificity for position 8 of the viral peptide, which is the sole discriminator of self versus nonself. Despite the evolutionary divergence of MHC class Ia and class Ib molecules, the structure of the T cell receptor-MHC class Ib complex was very similar to that of conventional T cell receptor-MHC class Ia complexes. These results emphasize the evolutionary 'ambiguity' of HLA-E, which not only interacts with innate immune receptors but also has the functional capacity to mediate virus-specific cytotoxic T lymphocyte responses during adaptive immunity.

About this Structure

2ESV is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis for a major histocompatibility complex class Ib-restricted T cell response., Hoare HL, Sullivan LC, Pietra G, Clements CS, Lee EJ, Ely LK, Beddoe T, Falco M, Kjer-Nielsen L, Reid HH, McCluskey J, Moretta L, Rossjohn J, Brooks AG, Nat Immunol. 2006 Mar;7(3):256-64. Epub 2006 Feb 12. PMID:16474394

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