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| <StructureSection load='4c2x' size='340' side='right'caption='[[4c2x]], [[Resolution|resolution]] 2.33Å' scene=''> | | <StructureSection load='4c2x' size='340' side='right'caption='[[4c2x]], [[Resolution|resolution]] 2.33Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4c2x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C2X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C2X FirstGlance]. <br> | | <table><tr><td colspan='2'>[[4c2x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C2X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C2X FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NHW:2-OXOPENTADECYL-COA'>NHW</scene></td></tr> | | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NHW:2-OXOPENTADECYL-COA'>NHW</scene></td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c2y|4c2y]], [[4c2z|4c2z]]</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=4c2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c2x OCA], [https://pdbe.org/4c2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c2x RCSB], [https://www.ebi.ac.uk/pdbsum/4c2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c2x ProSAT]</span></td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycylpeptide_N-tetradecanoyltransferase Glycylpeptide N-tetradecanoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.97 2.3.1.97] </span></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=4c2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c2x OCA], [http://pdbe.org/4c2x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c2x RCSB], [http://www.ebi.ac.uk/pdbsum/4c2x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c2x ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/NMT2_HUMAN NMT2_HUMAN]] Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins. | | [[https://www.uniprot.org/uniprot/NMT2_HUMAN NMT2_HUMAN]] Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins. |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Protein N-myristoylation is a ubiquitous co- and post-translational modification that has been implicated in the development and progression of a range of human diseases. Here, we report the global N-myristoylated proteome in human cells determined using quantitative chemical proteomics combined with potent and specific human N-myristoyltransferase (NMT) inhibition. Global quantification of N-myristoylation during normal growth or apoptosis allowed the identification of >100 N-myristoylated proteins, >95% of which are identified for the first time at endogenous levels. Furthermore, quantitative dose response for inhibition of N-myristoylation is determined for >70 substrates simultaneously across the proteome. Small-molecule inhibition through a conserved substrate-binding pocket is also demonstrated by solving the crystal structures of inhibitor-bound NMT1 and NMT2. The presented data substantially expand the known repertoire of co- and post-translational N-myristoylation in addition to validating tools for the pharmacological inhibition of NMT in living cells.
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| Global profiling of co- and post-translationally N-myristoylated proteomes in human cells.,Thinon E, Serwa RA, Broncel M, Brannigan JA, Brassat U, Wright MH, Heal WP, Wilkinson AJ, Mann DJ, Tate EW Nat Commun. 2014 Sep 26;5:4919. doi: 10.1038/ncomms5919. PMID:25255805<ref>PMID:25255805</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 4c2x" style="background-color:#fffaf0;"></div>
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| == References ==
| |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Glycylpeptide N-tetradecanoyltransferase]] | | [[Category: Homo sapiens]] |
| [[Category: Human]]
| |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Brannigan, J A]] | | [[Category: Brannigan JA]] |
| [[Category: Brassat, U]] | | [[Category: Brassat U]] |
| [[Category: Heal, W P]] | | [[Category: Heal WP]] |
| [[Category: Mann, D J]] | | [[Category: Mann DJ]] |
| [[Category: Serwa, R A]] | | [[Category: Serwa RA]] |
| [[Category: Tate, E W]] | | [[Category: Tate EW]] |
| [[Category: Thinon, E]] | | [[Category: Thinon E]] |
| [[Category: Wilkinson, A J]] | | [[Category: Wilkinson AJ]] |
| [[Category: Wright, M H]] | | [[Category: Wright MH]] |
| [[Category: Myristoylation]]
| |
| [[Category: Transferase]]
| |