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==Human N-myristoyltransferase isoform 2 (NMT2)== | ==Human N-myristoyltransferase isoform 2 (NMT2)== | ||
<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. 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 [ | <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><td class="sblockLbl"><b>[[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.33Å</td></tr> | ||
<tr><td class="sblockLbl"><b>[[ | <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='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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </table> | ||
<table> | == Function == | ||
[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;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4c2x" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Brannigan | [[Category: Large Structures]] | ||
[[Category: Brassat | [[Category: Brannigan JA]] | ||
[[Category: Heal | [[Category: Brassat U]] | ||
[[Category: Mann | [[Category: Heal WP]] | ||
[[Category: Serwa | [[Category: Mann DJ]] | ||
[[Category: Tate | [[Category: Serwa RA]] | ||
[[Category: Thinon | [[Category: Tate EW]] | ||
[[Category: Wilkinson | [[Category: Thinon E]] | ||
[[Category: Wright | [[Category: Wilkinson AJ]] | ||
[[Category: Wright MH]] | |||
Latest revision as of 15:02, 20 December 2023
Human N-myristoyltransferase isoform 2 (NMT2)Human N-myristoyltransferase isoform 2 (NMT2)
Structural highlights
FunctionNMT2_HUMAN Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins. Publication Abstract from PubMedProtein 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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