5ggj
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with Man-alpha-pNP== | |
| - | + | <StructureSection load='5ggj' size='340' side='right' caption='[[5ggj]], [[Resolution|resolution]] 1.42Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5ggj]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GGJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GGJ FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PNA:4-NITROPHENYL-ALPHA-D-MANNOPYRANOSIDE'>PNA</scene></td></tr> | |
| - | [[Category: | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ggf|5ggf]], [[5ggg|5ggg]], [[5ggi|5ggi]], [[5ggk|5ggk]], [[5ggl|5ggl]], [[5ggn|5ggn]], [[5ggo|5ggo]], [[5ggp|5ggp]]</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ggj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ggj OCA], [http://pdbe.org/5ggj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ggj RCSB], [http://www.ebi.ac.uk/pdbsum/5ggj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ggj ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/PMGT1_HUMAN PMGT1_HUMAN]] Walker-Warburg syndrome;Autosomal recessive limb-girdle muscular dystrophy type 2O;Congenital muscular dystrophy with cerebellar involvement;Muscle-eye-brain disease. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PMGT1_HUMAN PMGT1_HUMAN]] Participates in O-mannosyl glycosylation. May be responsible for the synthesis of the GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr moiety on alpha-dystroglycan and other O-mannosylated proteins. Is specific for alpha linked terminal mannose and does not have MGAT3, MGAT4, MGAT5, MGAT7 or MGAT8 activity.<ref>PMID:11709191</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Kato, R]] | ||
[[Category: Kuwabara, N]] | [[Category: Kuwabara, N]] | ||
| - | [[Category: Kato, R]] | ||
[[Category: Senda, T]] | [[Category: Senda, T]] | ||
| + | [[Category: Alpha-dystroglycan]] | ||
| + | [[Category: Glycosyltransferease]] | ||
| + | [[Category: O-mannosylation]] | ||
| + | [[Category: Sugar binding protein]] | ||
Revision as of 16:25, 10 August 2016
Crystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with Man-alpha-pNP
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