4c2x: Difference between revisions

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-'''Unreleased structure'''
-The entry 4c2x is ON HOLD
+==Human N-myristoyltransferase isoform 2 (NMT2)==
+<StructureSection load='4c2x' size='340' side='right'caption='[[4c2x]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
+== Structural highlights ==
+<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.33&#8491;</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='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>
+</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 &gt;100 N-myristoylated proteins, &gt;95% of which are identified for the first time at endogenous levels. Furthermore, quantitative dose response for inhibition of N-myristoylation is determined for &gt;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.
-Authors: Thinon, E., Serwa, R.A., Brannigan, J.A., Brassat, U., Wright, M.H., Heal, W.P., Wilkinson, A.J., Mann, D.J., Tate, E.W.
+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>
-Description: Human N-myristoyltransferase isoform 2 (NMT2)
+From MEDLINE&reg;/PubMed&reg;, 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__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Brannigan JA]]
+[[Category: Brassat U]]
+[[Category: Heal WP]]
+[[Category: Mann DJ]]
+[[Category: Serwa RA]]
+[[Category: Tate EW]]
+[[Category: Thinon E]]
+[[Category: Wilkinson AJ]]
+[[Category: Wright MH]]