5kxq

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'''Unreleased structure'''
 
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The entry 5kxq is ON HOLD until Paper Publication
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==mouse POFUT1 in complex with GDP==
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<StructureSection load='5kxq' size='340' side='right' caption='[[5kxq]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5kxq]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KXQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KXQ FirstGlance]. <br>
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Description:
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kxh|5kxh]], [[5ky0|5ky0]], [[5ky2|5ky2]], [[5ky3|5ky3]], [[5ky4|5ky4]], [[5ky5|5ky5]], [[5ky7|5ky7]], [[5ky8|5ky8]], [[5ky9|5ky9]]</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide-O-fucosyltransferase Peptide-O-fucosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.221 2.4.1.221] </span></td></tr>
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<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=5kxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kxq OCA], [http://pdbe.org/5kxq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kxq RCSB], [http://www.ebi.ac.uk/pdbsum/5kxq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kxq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/OFUT1_MOUSE OFUT1_MOUSE]] Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines. Specifically uses GDP-fucose as donor substrate and proper disulfide pairing of the substrate EGF domains is required for fucose transfer. Plays a crucial role in NOTCH signaling. Initial fucosylation of NOTCH by POFUT1 generates a substrate for FRINGE/RFNG, an acetylglucosaminyltransferase that can then extend the fucosylation on the NOTCH EGF repeats. This extended fucosylation is required for optimal ligand binding and canonical NOTCH signaling induced by DLL1 or JAGGED1. Fucosylates AGRN and determines its ability to cluster acetylcholine receptors (AChRs).<ref>PMID:12697902</ref> <ref>PMID:18775496</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Peptide-O-fucosyltransferase]]
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[[Category: Li, Z]]
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[[Category: Rini, J M]]
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[[Category: Glycosyltransferase o-fucosyltransferase gt-b inverting]]
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[[Category: Transferase]]

Revision as of 15:47, 17 May 2017

mouse POFUT1 in complex with GDP

5kxq, resolution 1.90Å

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