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== | ==Structure of the catalytic domain of mouse Manic Fringe in complex with UDP and manganese== | ||
Fringe proteins are beta1,3-N-acetylglucosaminyltransferases that modify | <StructureSection load='2j0b' size='340' side='right'caption='[[2j0b]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2j0b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J0B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J0B FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2j0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j0b OCA], [https://pdbe.org/2j0b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j0b RCSB], [https://www.ebi.ac.uk/pdbsum/2j0b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j0b ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MFNG_MOUSE MFNG_MOUSE] Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules (PubMed:10935626). Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in inhibition of NOTCH1 activation by JAG1 and enhancement of NOTCH1 activation by DLL1 via an increase in its binding to DLL1 (PubMed:10935626, PubMed:28089369).<ref>PMID:10935626</ref> <ref>PMID:28089369</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j0/2j0b_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2j0b ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Fringe proteins are beta1,3-N-acetylglucosaminyltransferases that modify Notch receptors, altering their ligand-binding specificity to regulate Notch signaling in development. We present the crystal structure of mouse Manic Fringe bound to UDP and manganese. The structure reveals amino acid residues involved in recognition of donor substrates and catalysis, and a putative binding pocket for acceptor substrates. Mutations of several invariant residues in this pocket impair Fringe activity in vivo. | |||
Structural insights into the Notch-modifying glycosyltransferase Fringe.,Jinek M, Chen YW, Clausen H, Cohen SM, Conti E Nat Struct Mol Biol. 2006 Oct;13(10):945-6. Epub 2006 Sep 10. PMID:16964258<ref>PMID:16964258</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 2j0b" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[O-GlcNAc transferase 3D structures|O-GlcNAc transferase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Chen Y-W]] | |||
[[Category: Clausen H]] | |||
[[Category: Chen | [[Category: Cohen SM]] | ||
[[Category: Clausen | [[Category: Conti E]] | ||
[[Category: Cohen | [[Category: Jinek M]] | ||
[[Category: Conti | |||
[[Category: Jinek | |||
Latest revision as of 10:55, 23 October 2024
Structure of the catalytic domain of mouse Manic Fringe in complex with UDP and manganeseStructure of the catalytic domain of mouse Manic Fringe in complex with UDP and manganese
Structural highlights
FunctionMFNG_MOUSE Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules (PubMed:10935626). Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in inhibition of NOTCH1 activation by JAG1 and enhancement of NOTCH1 activation by DLL1 via an increase in its binding to DLL1 (PubMed:10935626, PubMed:28089369).[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedFringe proteins are beta1,3-N-acetylglucosaminyltransferases that modify Notch receptors, altering their ligand-binding specificity to regulate Notch signaling in development. We present the crystal structure of mouse Manic Fringe bound to UDP and manganese. The structure reveals amino acid residues involved in recognition of donor substrates and catalysis, and a putative binding pocket for acceptor substrates. Mutations of several invariant residues in this pocket impair Fringe activity in vivo. Structural insights into the Notch-modifying glycosyltransferase Fringe.,Jinek M, Chen YW, Clausen H, Cohen SM, Conti E Nat Struct Mol Biol. 2006 Oct;13(10):945-6. Epub 2006 Sep 10. PMID:16964258[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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