1g7q

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(New page: 200px<br /><applet load="1g7q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g7q, resolution 1.60&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1g7q.jpg|left|200px]]<br /><applet load="1g7q" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1g7q.jpg|left|200px]]<br /><applet load="1g7q" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1g7q, resolution 1.60&Aring;" />
caption="1g7q, resolution 1.60&Aring;" />
'''CRYSTAL STRUCTURE OF MHC CLASS I H-2KB HEAVY CHAIN COMPLEXED WITH BETA-2 MICROGLOBULIN AND MUC1 VNTR PEPTIDE SAPDTRPA'''<br />
'''CRYSTAL STRUCTURE OF MHC CLASS I H-2KB HEAVY CHAIN COMPLEXED WITH BETA-2 MICROGLOBULIN AND MUC1 VNTR PEPTIDE SAPDTRPA'''<br />
==Overview==
==Overview==
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Peptides bind with high affinity to MHC class I molecules by anchoring, certain side-chains (anchors) into specificity pockets in the MHC, peptide-binding groove. Peptides that do not contain these canonical, anchor residues normally have low affinity, resulting in impaired pMHC, stability and loss of immunogenicity. Here, we report the crystal, structure at 1.6 A resolution of an immunogenic, low-affinity peptide from, the tumor-associated antigen MUC1, bound to H-2Kb. Stable binding is still, achieved despite small, non-canonical residues in the C and F anchor, pockets. This structure reveals how low-affinity peptides can be utilized, in the design of novel peptide-based tumor vaccines. The molecular, interactions elucidated in this non-canonical low-affinity peptide MHC, complex should help uncover additional immunogenic peptides from primary, protein sequences and aid in the design of alternative approaches for, T-cell vaccines.
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Peptides bind with high affinity to MHC class I molecules by anchoring certain side-chains (anchors) into specificity pockets in the MHC peptide-binding groove. Peptides that do not contain these canonical anchor residues normally have low affinity, resulting in impaired pMHC stability and loss of immunogenicity. Here, we report the crystal structure at 1.6 A resolution of an immunogenic, low-affinity peptide from the tumor-associated antigen MUC1, bound to H-2Kb. Stable binding is still achieved despite small, non-canonical residues in the C and F anchor pockets. This structure reveals how low-affinity peptides can be utilized in the design of novel peptide-based tumor vaccines. The molecular interactions elucidated in this non-canonical low-affinity peptide MHC complex should help uncover additional immunogenic peptides from primary protein sequences and aid in the design of alternative approaches for T-cell vaccines.
==About this Structure==
==About this Structure==
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1G7Q 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 NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G7Q OCA].
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1G7Q 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=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G7Q OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Apostolopoulos, V.]]
[[Category: Apostolopoulos, V.]]
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[[Category: Corper, A.L.]]
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[[Category: Corper, A L.]]
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[[Category: McKenzie, I.F.]]
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[[Category: McKenzie, I F.]]
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[[Category: Pietersz, G.A.]]
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[[Category: Pietersz, G A.]]
[[Category: Teyton, L.]]
[[Category: Teyton, L.]]
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[[Category: Wilson, I.A.]]
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[[Category: Wilson, I A.]]
[[Category: Yu, M.]]
[[Category: Yu, M.]]
[[Category: NAG]]
[[Category: NAG]]
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[[Category: vntr]]
[[Category: vntr]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:47:24 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:47:03 2008''

Revision as of 10:47, 21 February 2008

Image:1g7q.jpg

1g7q, resolution 1.60Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF MHC CLASS I H-2KB HEAVY CHAIN COMPLEXED WITH BETA-2 MICROGLOBULIN AND MUC1 VNTR PEPTIDE SAPDTRPA

Overview

Peptides bind with high affinity to MHC class I molecules by anchoring certain side-chains (anchors) into specificity pockets in the MHC peptide-binding groove. Peptides that do not contain these canonical anchor residues normally have low affinity, resulting in impaired pMHC stability and loss of immunogenicity. Here, we report the crystal structure at 1.6 A resolution of an immunogenic, low-affinity peptide from the tumor-associated antigen MUC1, bound to H-2Kb. Stable binding is still achieved despite small, non-canonical residues in the C and F anchor pockets. This structure reveals how low-affinity peptides can be utilized in the design of novel peptide-based tumor vaccines. The molecular interactions elucidated in this non-canonical low-affinity peptide MHC complex should help uncover additional immunogenic peptides from primary protein sequences and aid in the design of alternative approaches for T-cell vaccines.

About this Structure

1G7Q is a Protein complex structure of sequences from Mus musculus with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of a non-canonical low-affinity peptide complexed with MHC class I: a new approach for vaccine design., Apostolopoulos V, Yu M, Corper AL, Teyton L, Pietersz GA, McKenzie IF, Wilson IA, Plebanski M, J Mol Biol. 2002 May 17;318(5):1293-305. PMID:12083518

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