1k2d

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(New page: 200px<br /><applet load="1k2d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k2d, resolution 2.2&Aring;" /> '''Crystal structure of ...)
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[[Image:1k2d.jpg|left|200px]]<br /><applet load="1k2d" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1k2d.jpg|left|200px]]<br /><applet load="1k2d" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1k2d, resolution 2.2&Aring;" />
caption="1k2d, resolution 2.2&Aring;" />
'''Crystal structure of the autoimmune MHC class II I-Au complexed with myelin basic protein 1-11 at 2.2A'''<br />
'''Crystal structure of the autoimmune MHC class II I-Au complexed with myelin basic protein 1-11 at 2.2A'''<br />
==Overview==
==Overview==
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Murine experimental allergic encephalomyelitis (EAE) is a useful model for, the demyelinating, autoimmune disease multiple sclerosis. In the EAE, system, the immunodominant N-terminal epitope of myelin basic protein, (MBP) is an unusually short, weakly binding peptide antigen which elicits, highly biased TCR chain usage. In the 2.2 A crystal structure of, I-A(u)/MBP1-11 complex, only MBP residues 1-7 are bound toward one end of, the peptide binding cleft. The fourth residue of MBP1-11 is located in an, incompatible p6 pocket of I-A(u), thus explaining the short half-life of, I-A(u) complexed with Ac1-11. MBP peptides extended at the C terminus of, Ac1-11 result in dramatic affinity increases, likely attributed to, register shifting to a higher affinity cryptic epitope, which could, potentially mask the presentation of the immunodominant MBP1-11 peptide, during thymic education.
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Murine experimental allergic encephalomyelitis (EAE) is a useful model for the demyelinating, autoimmune disease multiple sclerosis. In the EAE system, the immunodominant N-terminal epitope of myelin basic protein (MBP) is an unusually short, weakly binding peptide antigen which elicits highly biased TCR chain usage. In the 2.2 A crystal structure of I-A(u)/MBP1-11 complex, only MBP residues 1-7 are bound toward one end of the peptide binding cleft. The fourth residue of MBP1-11 is located in an incompatible p6 pocket of I-A(u), thus explaining the short half-life of I-A(u) complexed with Ac1-11. MBP peptides extended at the C terminus of Ac1-11 result in dramatic affinity increases, likely attributed to register shifting to a higher affinity cryptic epitope, which could potentially mask the presentation of the immunodominant MBP1-11 peptide during thymic education.
==About this Structure==
==About this Structure==
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1K2D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NDG and NAG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K2D OCA].
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1K2D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NDG:'>NDG</scene> and <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K2D OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Garcia, K.C.]]
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[[Category: Garcia, K C.]]
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[[Category: He, X.L.]]
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[[Category: He, X L.]]
[[Category: Radu, C.]]
[[Category: Radu, C.]]
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[[Category: Ward, E.S.]]
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[[Category: Ward, E S.]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: NDG]]
[[Category: NDG]]
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[[Category: unique register]]
[[Category: unique register]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:47:31 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:29:19 2008''

Revision as of 11:29, 21 February 2008


1k2d, resolution 2.2Å

Drag the structure with the mouse to rotate

Crystal structure of the autoimmune MHC class II I-Au complexed with myelin basic protein 1-11 at 2.2A

Overview

Murine experimental allergic encephalomyelitis (EAE) is a useful model for the demyelinating, autoimmune disease multiple sclerosis. In the EAE system, the immunodominant N-terminal epitope of myelin basic protein (MBP) is an unusually short, weakly binding peptide antigen which elicits highly biased TCR chain usage. In the 2.2 A crystal structure of I-A(u)/MBP1-11 complex, only MBP residues 1-7 are bound toward one end of the peptide binding cleft. The fourth residue of MBP1-11 is located in an incompatible p6 pocket of I-A(u), thus explaining the short half-life of I-A(u) complexed with Ac1-11. MBP peptides extended at the C terminus of Ac1-11 result in dramatic affinity increases, likely attributed to register shifting to a higher affinity cryptic epitope, which could potentially mask the presentation of the immunodominant MBP1-11 peptide during thymic education.

About this Structure

1K2D is a Protein complex structure of sequences from Mus musculus with and as ligands. Full crystallographic information is available from OCA.

Reference

Structural snapshot of aberrant antigen presentation linked to autoimmunity: the immunodominant epitope of MBP complexed with I-Au., He XL, Radu C, Sidney J, Sette A, Ward ES, Garcia KC, Immunity. 2002 Jul;17(1):83-94. PMID:12150894

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