1xz0

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(New page: 200px<br /> <applet load="1xz0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xz0, resolution 2.80&Aring;" /> '''Crystal structure o...)
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[[Image:1xz0.gif|left|200px]]<br />
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[[Image:1xz0.gif|left|200px]]<br /><applet load="1xz0" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1xz0" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1xz0, resolution 2.80&Aring;" />
caption="1xz0, resolution 2.80&Aring;" />
'''Crystal structure of CD1a in complex with a synthetic mycobactin lipopeptide'''<br />
'''Crystal structure of CD1a in complex with a synthetic mycobactin lipopeptide'''<br />
==Overview==
==Overview==
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CD1a is expressed on Langerhans cells (LCs) and dendritic cells (DCs), where it mediates T cell recognition of glycolipid and lipopeptide, antigens that contain either one or two alkyl chains. We demonstrate here, that CD1a-restricted T cells can discriminate the peptide component of, didehydroxymycobactin lipopeptides. Structure analysis of CD1a, cocrystallized with a synthetic mycobactin lipopeptide at 2.8 A resolution, further reveals that the single alkyl chain is inserted deep within the A', pocket of the groove, whereas its two peptidic branches protrude along the, F' pocket to the outer, alpha-helical surface of CD1a for recognition by, the TCR. Remarkably, the cyclized lysine branch of the peptide moiety lies, in the shallow F' pocket in a conformation that closely mimics that of the, alkyl chain in the CD1a-sulfatide structure. Thus, this structural study, illustrates how a single chain lipid can be presented by CD1 and that the, peptide moiety of the lipopeptide is recognized by the TCR.
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CD1a is expressed on Langerhans cells (LCs) and dendritic cells (DCs), where it mediates T cell recognition of glycolipid and lipopeptide antigens that contain either one or two alkyl chains. We demonstrate here that CD1a-restricted T cells can discriminate the peptide component of didehydroxymycobactin lipopeptides. Structure analysis of CD1a cocrystallized with a synthetic mycobactin lipopeptide at 2.8 A resolution further reveals that the single alkyl chain is inserted deep within the A' pocket of the groove, whereas its two peptidic branches protrude along the F' pocket to the outer, alpha-helical surface of CD1a for recognition by the TCR. Remarkably, the cyclized lysine branch of the peptide moiety lies in the shallow F' pocket in a conformation that closely mimics that of the alkyl chain in the CD1a-sulfatide structure. Thus, this structural study illustrates how a single chain lipid can be presented by CD1 and that the peptide moiety of the lipopeptide is recognized by the TCR.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1XZ0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with JH0 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XZ0 OCA].
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1XZ0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=JH0:'>JH0</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XZ0 OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Bowden, T.A.]]
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[[Category: Bowden, T A.]]
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[[Category: Cheng, T.Y.]]
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[[Category: Cheng, T Y.]]
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[[Category: Costello, C.E.]]
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[[Category: Costello, C E.]]
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[[Category: Crispin, M.D.]]
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[[Category: Crispin, M D.]]
[[Category: Hu, J.]]
[[Category: Hu, J.]]
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[[Category: Miller, M.J.]]
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[[Category: Miller, M J.]]
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[[Category: Moody, D.B.]]
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[[Category: Moody, D B.]]
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[[Category: Wilson, I.A.]]
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[[Category: Wilson, I A.]]
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[[Category: Young, D.C.]]
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[[Category: Young, D C.]]
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[[Category: Zajonc, D.M.]]
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[[Category: Zajonc, D M.]]
[[Category: JH0]]
[[Category: JH0]]
[[Category: beta sheet platform]]
[[Category: beta sheet platform]]
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[[Category: protein-lipopeptide complex]]
[[Category: protein-lipopeptide complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:12:32 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:00:07 2008''

Revision as of 14:00, 21 February 2008


1xz0, resolution 2.80Å

Drag the structure with the mouse to rotate

Crystal structure of CD1a in complex with a synthetic mycobactin lipopeptide

Contents

Overview

CD1a is expressed on Langerhans cells (LCs) and dendritic cells (DCs), where it mediates T cell recognition of glycolipid and lipopeptide antigens that contain either one or two alkyl chains. We demonstrate here that CD1a-restricted T cells can discriminate the peptide component of didehydroxymycobactin lipopeptides. Structure analysis of CD1a cocrystallized with a synthetic mycobactin lipopeptide at 2.8 A resolution further reveals that the single alkyl chain is inserted deep within the A' pocket of the groove, whereas its two peptidic branches protrude along the F' pocket to the outer, alpha-helical surface of CD1a for recognition by the TCR. Remarkably, the cyclized lysine branch of the peptide moiety lies in the shallow F' pocket in a conformation that closely mimics that of the alkyl chain in the CD1a-sulfatide structure. Thus, this structural study illustrates how a single chain lipid can be presented by CD1 and that the peptide moiety of the lipopeptide is recognized by the TCR.

Disease

Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[109700]

About this Structure

1XZ0 is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Molecular mechanism of lipopeptide presentation by CD1a., Zajonc DM, Crispin MD, Bowden TA, Young DC, Cheng TY, Hu J, Costello CE, Rudd PM, Dwek RA, Miller MJ, Brenner MB, Moody DB, Wilson IA, Immunity. 2005 Feb;22(2):209-19. PMID:15723809

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