1n5a

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(New page: 200px<br /><applet load="1n5a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n5a, resolution 2.85&Aring;" /> '''Crystal structure of...)
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[[Image:1n5a.gif|left|200px]]<br /><applet load="1n5a" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1n5a.gif|left|200px]]<br /><applet load="1n5a" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1n5a, resolution 2.85&Aring;" />
caption="1n5a, resolution 2.85&Aring;" />
'''Crystal structure of the Murine class I Major Histocompatibility Complex of H-2DB, B2-Microglobulin, and A 9-Residue immunodominant peptide epitope gp33 derived from LCMV'''<br />
'''Crystal structure of the Murine class I Major Histocompatibility Complex of H-2DB, B2-Microglobulin, and A 9-Residue immunodominant peptide epitope gp33 derived from LCMV'''<br />
==Overview==
==Overview==
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LCMV infection of H-2(b) mice generates a CD8(+) CTL response mainly, directed toward three immunodominant epitopes. One of these, gp33, is, presented by both H-2D(b) and H-2K(b) MHC class I molecules. The virus can, escape immune recognition in the context of both these MHC class I, molecules through single mutations of the peptide. In order to understand, the underlying structural mechanism, we determined the crystal structures, of both complexes. The structures reveal that the peptide is presented in, two diametrically opposed manners by H-2D(b) and H-2K(b), with residues, used as anchor positions in one MHC class I molecule interacting with the, TCR in the other. Importantly, the peptide's N-terminal residue p1K, protrudes from the binding cleft in H-2K(b). We present structural, evidence that explains the functional consequences of single mutations, found in escape variants.
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LCMV infection of H-2(b) mice generates a CD8(+) CTL response mainly directed toward three immunodominant epitopes. One of these, gp33, is presented by both H-2D(b) and H-2K(b) MHC class I molecules. The virus can escape immune recognition in the context of both these MHC class I molecules through single mutations of the peptide. In order to understand the underlying structural mechanism, we determined the crystal structures of both complexes. The structures reveal that the peptide is presented in two diametrically opposed manners by H-2D(b) and H-2K(b), with residues used as anchor positions in one MHC class I molecule interacting with the TCR in the other. Importantly, the peptide's N-terminal residue p1K protrudes from the binding cleft in H-2K(b). We present structural evidence that explains the functional consequences of single mutations found in escape variants.
==About this Structure==
==About this Structure==
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1N5A is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N5A OCA].
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1N5A is a [http://en.wikipedia.org/wiki/Protein_complex 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=1N5A OCA].
==Reference==
==Reference==
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[[Category: Achour, A.]]
[[Category: Achour, A.]]
[[Category: Grufman, P.]]
[[Category: Grufman, P.]]
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[[Category: Harris, R.A.]]
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[[Category: Harris, R A.]]
[[Category: Karre, K.]]
[[Category: Karre, K.]]
[[Category: Levitsky, V.]]
[[Category: Levitsky, V.]]
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[[Category: Odeberg, J.]]
[[Category: Odeberg, J.]]
[[Category: Sandalova, T.]]
[[Category: Sandalova, T.]]
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[[Category: Sandberg, J.K.]]
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[[Category: Sandberg, J K.]]
[[Category: Schneider, G.]]
[[Category: Schneider, G.]]
[[Category: immunodominant epitope]]
[[Category: immunodominant epitope]]
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[[Category: viral escape]]
[[Category: viral escape]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:58:25 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:02:25 2008''

Revision as of 12:02, 21 February 2008


1n5a, resolution 2.85Å

Drag the structure with the mouse to rotate

Crystal structure of the Murine class I Major Histocompatibility Complex of H-2DB, B2-Microglobulin, and A 9-Residue immunodominant peptide epitope gp33 derived from LCMV

Overview

LCMV infection of H-2(b) mice generates a CD8(+) CTL response mainly directed toward three immunodominant epitopes. One of these, gp33, is presented by both H-2D(b) and H-2K(b) MHC class I molecules. The virus can escape immune recognition in the context of both these MHC class I molecules through single mutations of the peptide. In order to understand the underlying structural mechanism, we determined the crystal structures of both complexes. The structures reveal that the peptide is presented in two diametrically opposed manners by H-2D(b) and H-2K(b), with residues used as anchor positions in one MHC class I molecule interacting with the TCR in the other. Importantly, the peptide's N-terminal residue p1K protrudes from the binding cleft in H-2K(b). We present structural evidence that explains the functional consequences of single mutations found in escape variants.

About this Structure

1N5A is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

A structural basis for LCMV immune evasion: subversion of H-2D(b) and H-2K(b) presentation of gp33 revealed by comparative crystal structure.Analyses., Achour A, Michaelsson J, Harris RA, Odeberg J, Grufman P, Sandberg JK, Levitsky V, Karre K, Sandalova T, Schneider G, Immunity. 2002 Dec;17(6):757-68. PMID:12479822

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