2hrl
From Proteopedia
(New page: 200px<br /> <applet load="2hrl" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hrl, resolution 1.85Å" /> '''Siglec-7 in complex...) |
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| - | [[Image:2hrl.gif|left|200px]]<br /> | + | [[Image:2hrl.gif|left|200px]]<br /><applet load="2hrl" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2hrl" size=" | + | |
caption="2hrl, resolution 1.85Å" /> | caption="2hrl, resolution 1.85Å" /> | ||
'''Siglec-7 in complex with GT1b'''<br /> | '''Siglec-7 in complex with GT1b'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The siglecs are a group of mammalian sialic acid binding receptors | + | The siglecs are a group of mammalian sialic acid binding receptors expressed predominantly in the immune system. The CD33-related siglecs show complex recognition patterns for sialylated glycans. Siglec-7 shows a preference for alpha(2,8)-disialylated ligands and provides a structural template for studying the key interactions that drive this selectivity. We have co-crystallized Siglec-7 with a synthetic oligosaccharide corresponding to the alpha(2,8)-disialylated ganglioside GT1b. The crystal structure of the complex offers a first glimpse into how this important family of lectins binds the structurally diverse gangliosides. The structure reveals that the C-C' loop, a region implicated in previous studies as driving siglec specificity, undergoes a dramatic conformational shift, allowing it to interact with the underlying neutral glycan core of the ganglioside. The structural data in combination with mutagenesis studies show that binding of the ganglioside is driven by extensive hydrophobic contacts together with key polar interactions and that the binding site structure is complementary to preferred solution conformations of GT1b. |
==About this Structure== | ==About this Structure== | ||
| - | 2HRL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG and CEQ as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2HRL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=CEQ:'>CEQ</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HRL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Aalten, D | + | [[Category: Aalten, D M.F van.]] |
[[Category: Attrill, H.]] | [[Category: Attrill, H.]] | ||
| - | [[Category: Crocker, P | + | [[Category: Crocker, P R.]] |
[[Category: Imamura, A.]] | [[Category: Imamura, A.]] | ||
[[Category: Kiso, M.]] | [[Category: Kiso, M.]] | ||
| - | [[Category: Sharma, R | + | [[Category: Sharma, R S.]] |
[[Category: CEQ]] | [[Category: CEQ]] | ||
[[Category: NAG]] | [[Category: NAG]] | ||
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[[Category: siglec-7]] | [[Category: siglec-7]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:45:02 2008'' |
Revision as of 15:45, 21 February 2008
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Siglec-7 in complex with GT1b
Overview
The siglecs are a group of mammalian sialic acid binding receptors expressed predominantly in the immune system. The CD33-related siglecs show complex recognition patterns for sialylated glycans. Siglec-7 shows a preference for alpha(2,8)-disialylated ligands and provides a structural template for studying the key interactions that drive this selectivity. We have co-crystallized Siglec-7 with a synthetic oligosaccharide corresponding to the alpha(2,8)-disialylated ganglioside GT1b. The crystal structure of the complex offers a first glimpse into how this important family of lectins binds the structurally diverse gangliosides. The structure reveals that the C-C' loop, a region implicated in previous studies as driving siglec specificity, undergoes a dramatic conformational shift, allowing it to interact with the underlying neutral glycan core of the ganglioside. The structural data in combination with mutagenesis studies show that binding of the ganglioside is driven by extensive hydrophobic contacts together with key polar interactions and that the binding site structure is complementary to preferred solution conformations of GT1b.
About this Structure
2HRL is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Siglec-7 undergoes a major conformational change when complexed with the alpha(2,8)-disialylganglioside GT1b., Attrill H, Imamura A, Sharma RS, Kiso M, Crocker PR, van Aalten DM, J Biol Chem. 2006 Oct 27;281(43):32774-83. Epub 2006 Aug 8. PMID:16895906
Page seeded by OCA on Thu Feb 21 17:45:02 2008
Categories: Homo sapiens | Single protein | Aalten, D M.F van. | Attrill, H. | Crocker, P R. | Imamura, A. | Kiso, M. | Sharma, R S. | CEQ | NAG | Ganglioside | Ig-like domain | Siglec | Siglec-7
