2hrl

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|PDB= 2hrl |SIZE=350|CAPTION= <scene name='initialview01'>2hrl</scene>, resolution 1.85&Aring;
|PDB= 2hrl |SIZE=350|CAPTION= <scene name='initialview01'>2hrl</scene>, resolution 1.85&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=CEQ:ETHYL-TRIMETHYL-SILANE'>CEQ</scene>
+
|LIGAND= <scene name='pdbligand=CEQ:ETHYL-TRIMETHYL-SILANE'>CEQ</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NGA:N-ACETYL-D-GALACTOSAMINE'>NGA</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=[[1o7s|1O7S]], [[1o7v|1O7V]], [[2df3|2DF3]], [[2g5r|2G5R]]
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hrl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hrl OCA], [http://www.ebi.ac.uk/pdbsum/2hrl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hrl RCSB]</span>
}}
}}
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[[Category: Kiso, M.]]
[[Category: Kiso, M.]]
[[Category: Sharma, R S.]]
[[Category: Sharma, R S.]]
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[[Category: CEQ]]
 
-
[[Category: NAG]]
 
[[Category: ganglioside]]
[[Category: ganglioside]]
[[Category: ig-like domain]]
[[Category: ig-like domain]]
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[[Category: siglec-7]]
[[Category: siglec-7]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:20:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:34:23 2008''

Revision as of 00:34, 31 March 2008


PDB ID 2hrl

Drag the structure with the mouse to rotate
, resolution 1.85Å
Ligands: , , , , ,
Related: 1O7S, 1O7V, 2DF3, 2G5R


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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

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