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Name help_outline
3-O-{β-D-GlcA-(1→3)-[α-D-Xyl-(1→3)-β-D-GlcA-(1→3)]n-(1→4)-β-D-Xyl-(1→4)-Rib-ol-P-Rib-ol-P-3-β-D-GalNAc-(1→3)-β-D-GlcNAc-(1→4)-O-6-P-α-D-Man}-L-threonine residue
Identifier
CHEBI:177355
Charge
-6
Formula
(C11H15O10)n.C47H77N3O44P3
Search links
Involved in 3 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:17486Polymer name: 3-O-{β-D-GlcA-(1→[3)-α-D-Xyl-(1→3)-β-D-GlcA-(1→](n)-4)-β-D-Xyl-(1→4)-Rib-ol-P-Rib-ol-P-3-β-D-GalNAc-(1→3)-β-D-GlcNAc-(1→4)-O-6-P-α-D-Man}-L-Thr-[protein]Polymerization index help_outline nFormula C47H77N3O44P3(C11H15O10)nCharge (-5)(-1)nMol File for the polymer
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- Name help_outline 3'-phosphoadenylyl sulfate Identifier CHEBI:58339 Charge -4 Formula C10H11N5O13P2S InChIKeyhelp_outline GACDQMDRPRGCTN-KQYNXXCUSA-J SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OS([O-])(=O)=O)[C@@H](OP([O-])([O-])=O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 125 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Name help_outline
3-O-{3-S-β-D-GlcA-(1→3)-[α-D-Xyl-(1→3)-β-D-GlcA-(1→3)]n-(1→4)-β-D-Xyl-(1→4)-Rib-ol-P-Rib-ol-P-3-β-D-GalNAc-(1→3)-β-D-GlcNAc-(1→4)-O-6-P-α-D-Man}-L-threonine residue
Identifier
CHEBI:177363
Charge
-7
Formula
(C11H15O10)n.C47H76N3O47P3S
Search links
Involved in 1 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:17487Polymer name: 3-O-{O-3-S-β-D-GlcA-(1→[3)-α-D-Xyl-(1→3)-β-D-GlcA-(1→](n)-4)-β-D-Xyl-(1→4)-Rib-ol-P-Rib-ol-P-3-β-D-GalNAc-(1→3)-β-D-GlcNAc-(1→4)-O-6-P-α-D-Man}-L-Thr-[protein]Polymerization index help_outline nFormula C47H76N3O47P3S(C11H15O10)nCharge (-6)(-1)nMol File for the polymer
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- Name help_outline adenosine 3',5'-bisphosphate Identifier CHEBI:58343 Charge -4 Formula C10H11N5O10P2 InChIKeyhelp_outline WHTCPDAXWFLDIH-KQYNXXCUSA-J SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])([O-])=O)[C@@H](OP([O-])([O-])=O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 159 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,932 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:68304 | RHEA:68305 | RHEA:68306 | RHEA:68307 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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HNK-1 sulfotransferase modulates alpha-dystroglycan glycosylation by 3-O-sulfation of glucuronic acid on matriglycan.
Sheikh M.O., Venzke D., Anderson M.E., Yoshida-Moriguchi T., Glushka J.N., Nairn A.V., Galizzi M., Moremen K.W., Campbell K.P., Wells L.
Mutations in multiple genes required for proper O-mannosylation of α-dystroglycan are causal for congenital/limb-girdle muscular dystrophies and abnormal brain development in mammals. Previously, we and others further elucidated the functional O-mannose glycan structure that is terminated by matri ... >> More
Mutations in multiple genes required for proper O-mannosylation of α-dystroglycan are causal for congenital/limb-girdle muscular dystrophies and abnormal brain development in mammals. Previously, we and others further elucidated the functional O-mannose glycan structure that is terminated by matriglycan, [(-GlcA-β3-Xyl-α3-)n]. This repeating disaccharide serves as a receptor for proteins in the extracellular matrix. Here, we demonstrate in vitro that HNK-1 sulfotransferase (HNK-1ST/carbohydrate sulfotransferase) sulfates terminal glucuronyl residues of matriglycan at the 3-hydroxyl and prevents further matriglycan polymerization by the LARGE1 glycosyltransferase. While α-dystroglycan isolated from mouse heart and kidney is susceptible to exoglycosidase digestion of matriglycan, the functional, lower molecular weight α-dystroglycan detected in brain, where HNK-1ST expression is elevated, is resistant. Removal of the sulfate cap by a sulfatase facilitated dual-glycosidase digestion. Our data strongly support a tissue specific mechanism in which HNK-1ST regulates polymer length by competing with LARGE for the 3-position on the nonreducing GlcA of matriglycan. << Less