2h26

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="2h26" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h26, resolution 1.80&Aring;" /> '''human CD1b in compl...)
Line 1: Line 1:
-
[[Image:2h26.gif|left|200px]]<br />
+
[[Image:2h26.gif|left|200px]]<br /><applet load="2h26" size="350" color="white" frame="true" align="right" spinBox="true"
-
<applet load="2h26" size="450" color="white" frame="true" align="right" spinBox="true"
+
caption="2h26, resolution 1.80&Aring;" />
caption="2h26, resolution 1.80&Aring;" />
'''human CD1b in complex with endogenous phosphatidylcholine and spacer'''<br />
'''human CD1b in complex with endogenous phosphatidylcholine and spacer'''<br />
==Overview==
==Overview==
-
CD1 proteins present lipid antigens to T cells. The antigens are acquired, in the endosomal compartments. This raises the question of how the large, hydrophobic CD1 pockets are preserved between the moment of biosynthesis, in the endoplasmic reticulum and arrival to the endosomes. To address this, issue, the natural ligands associated with a soluble form of human CD1b, have been investigated. Using isoelectric focusing, native mass, spectrometry and resolving the crystal structure at 1.8 A resolution, we, found that human CD1b is simultaneously associated with endogenous, phosphatidylcholine (PC) and a 41-44 carbon atoms-long spacer molecule., The two lipids appear to work in concert to stabilize the CD1b groove, their combined size slightly exceeding the maximal groove capacity. We, propose that the spacer serves to prevent binding of ligands with long, lipid tails, whereas short-chain lipids might still displace the PC, which, is exposed at the groove entrance. The data presented herein explain how, the CD1b groove is preserved, and provide a rationale for the in vivo, antigen-binding properties of CD1b.
+
CD1 proteins present lipid antigens to T cells. The antigens are acquired in the endosomal compartments. This raises the question of how the large hydrophobic CD1 pockets are preserved between the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes. To address this issue, the natural ligands associated with a soluble form of human CD1b have been investigated. Using isoelectric focusing, native mass spectrometry and resolving the crystal structure at 1.8 A resolution, we found that human CD1b is simultaneously associated with endogenous phosphatidylcholine (PC) and a 41-44 carbon atoms-long spacer molecule. The two lipids appear to work in concert to stabilize the CD1b groove, their combined size slightly exceeding the maximal groove capacity. We propose that the spacer serves to prevent binding of ligands with long lipid tails, whereas short-chain lipids might still displace the PC, which is exposed at the groove entrance. The data presented herein explain how the CD1b groove is preserved, and provide a rationale for the in vivo antigen-binding properties of CD1b.
==Disease==
==Disease==
Line 11: Line 10:
==About this Structure==
==About this Structure==
-
2H26 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 SO4, 6PL, 6UL and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2H26 OCA].
+
2H26 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=SO4:'>SO4</scene>, <scene name='pdbligand=6PL:'>6PL</scene>, <scene name='pdbligand=6UL:'>6UL</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H26 OCA].
==Reference==
==Reference==
Line 17: Line 16:
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
-
[[Category: Garcia-Alles, L.F.]]
+
[[Category: Garcia-Alles, L F.]]
[[Category: Guillet, V.]]
[[Category: Guillet, V.]]
[[Category: Maveyraud, L.]]
[[Category: Maveyraud, L.]]
[[Category: Mourey, L.]]
[[Category: Mourey, L.]]
-
[[Category: Vallina, A.T.]]
+
[[Category: Vallina, A T.]]
[[Category: 6PL]]
[[Category: 6PL]]
[[Category: 6UL]]
[[Category: 6UL]]
Line 33: Line 32:
[[Category: phosphatidylcholine]]
[[Category: phosphatidylcholine]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:25:02 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:37:27 2008''

Revision as of 15:37, 21 February 2008


2h26, resolution 1.80Å

Drag the structure with the mouse to rotate

human CD1b in complex with endogenous phosphatidylcholine and spacer

Contents

Overview

CD1 proteins present lipid antigens to T cells. The antigens are acquired in the endosomal compartments. This raises the question of how the large hydrophobic CD1 pockets are preserved between the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes. To address this issue, the natural ligands associated with a soluble form of human CD1b have been investigated. Using isoelectric focusing, native mass spectrometry and resolving the crystal structure at 1.8 A resolution, we found that human CD1b is simultaneously associated with endogenous phosphatidylcholine (PC) and a 41-44 carbon atoms-long spacer molecule. The two lipids appear to work in concert to stabilize the CD1b groove, their combined size slightly exceeding the maximal groove capacity. We propose that the spacer serves to prevent binding of ligands with long lipid tails, whereas short-chain lipids might still displace the PC, which is exposed at the groove entrance. The data presented herein explain how the CD1b groove is preserved, and provide a rationale for the in vivo antigen-binding properties of CD1b.

Disease

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

About this Structure

2H26 is a Protein complex structure of sequences from Homo sapiens with , , and as ligands. Full crystallographic information is available from OCA.

Reference

Endogenous phosphatidylcholine and a long spacer ligand stabilize the lipid-binding groove of CD1b., Garcia-Alles LF, Versluis K, Maveyraud L, Vallina AT, Sansano S, Bello NF, Gober HJ, Guillet V, de la Salle H, Puzo G, Mori L, Heck AJ, De Libero G, Mourey L, EMBO J. 2006 Aug 9;25(15):3684-92. Epub 2006 Jul 27. PMID:16874306

Page seeded by OCA on Thu Feb 21 17:37:27 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools