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1zhb

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[[Image:1zhb.gif|left|200px]]<br /><applet load="1zhb" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1zhb.gif|left|200px]]
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caption="1zhb, resolution 2.70&Aring;" />
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'''Crystal Structure Of The Murine Class I Major Histocompatibility Complex Of H-2Db, B2-Microglobulin, and a 9-Residue Peptide Derived from rat dopamine beta-monooxigenase'''<br />
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{{Structure
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|PDB= 1zhb |SIZE=350|CAPTION= <scene name='initialview01'>1zhb</scene>, resolution 2.70&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY= [http://en.wikipedia.org/wiki/Dopamine_beta-monooxygenase Dopamine beta-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.1 1.14.17.1]
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|GENE= H2-D ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), B2M ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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}}
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'''Crystal Structure Of The Murine Class I Major Histocompatibility Complex Of H-2Db, B2-Microglobulin, and a 9-Residue Peptide Derived from rat dopamine beta-monooxigenase'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1ZHB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Active as [http://en.wikipedia.org/wiki/Dopamine_beta-monooxygenase Dopamine beta-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.1 1.14.17.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZHB OCA].
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1ZHB is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZHB OCA].
==Reference==
==Reference==
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A structural basis for CD8+ T cell-dependent recognition of non-homologous peptide ligands: implications for molecular mimicry in autoreactivity., Sandalova T, Michaelsson J, Harris RA, Odeberg J, Schneider G, Karre K, Achour A, J Biol Chem. 2005 Jul 22;280(29):27069-75. Epub 2005 Apr 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15845547 15845547]
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A structural basis for CD8+ T cell-dependent recognition of non-homologous peptide ligands: implications for molecular mimicry in autoreactivity., Sandalova T, Michaelsson J, Harris RA, Odeberg J, Schneider G, Karre K, Achour A, J Biol Chem. 2005 Jul 22;280(29):27069-75. Epub 2005 Apr 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15845547 15845547]
[[Category: Dopamine beta-monooxygenase]]
[[Category: Dopamine beta-monooxygenase]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: tcr-crossreactivity]]
[[Category: tcr-crossreactivity]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:15:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:35:27 2008''

Revision as of 13:35, 20 March 2008


PDB ID 1zhb

Drag the structure with the mouse to rotate
, resolution 2.70Å
Gene: H2-D (Mus musculus), B2M (Mus musculus)
Activity: Dopamine beta-monooxygenase, with EC number 1.14.17.1
Coordinates: save as pdb, mmCIF, xml



Crystal Structure Of The Murine Class I Major Histocompatibility Complex Of H-2Db, B2-Microglobulin, and a 9-Residue Peptide Derived from rat dopamine beta-monooxigenase


Overview

Molecular mimicry of self-epitopes by viral antigens is one possible pathogenic mechanism underlying induction of autoimmunity. A self-epitope, mDBM, derived from mouse dopamine beta-mono-oxygenase (KALYDYAPI) sharing 44% sequence identity with the lymphocytic choriomeningitis virus-derived immunodominant epitope gp33 (KAVYNFATC/M), has previously been identified as a cross-reactive self-ligand, presentation of which results in autoimmunity. A rat peptide homologue, rDBM (KALYNYAPI, 56% identity to gp33), which displayed similar properties to mDBM, has also been identified. We herein report the crystal structure of H-2Db.rDBM and a comparison with the crystal structures of the cross-reactive H-2Db.gp33 and non-cross-reactive H-2Db.gp33 (V3L) escape variant (KALYNFATM, 88% identity to gp33). Despite the large sequence disparity, rDBM and gp33 peptides are presented in nearly identical manners by H-2Db, with a striking juxtaposition of the central sections of both peptides from residues p3 to p7. The structural similarity provides H-2Db in complex with either a virus-derived or a dopamine beta-mono-oxygenase-derived peptide with a shared antigenic identity that conserves the positioning of the heavy chain and peptide residues that interact with the T cell receptor (TCR). This stands in contrast to the structure of H-2Db.gp33 (V3L), in which a single conserved mutation, also present in rDBM, induces large movements of both the peptide backbone and the side chains that interact with the TCR. The TCR-interacting surfaces of the H-2Db.rDBM and H-2Db.gp33 major histocompatibility complexes are very similar with regard to shape, topology, and charge distribution, providing a structural basis for CD8 T cell activation by molecular mimicry and potential subsequent development of autoreactivity.

About this Structure

1ZHB is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

A structural basis for CD8+ T cell-dependent recognition of non-homologous peptide ligands: implications for molecular mimicry in autoreactivity., Sandalova T, Michaelsson J, Harris RA, Odeberg J, Schneider G, Karre K, Achour A, J Biol Chem. 2005 Jul 22;280(29):27069-75. Epub 2005 Apr 21. PMID:15845547

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