4ufw: Difference between revisions
Jump to navigation
Jump to search
New page: '''Unreleased structure''' The entry 4ufw is ON HOLD until sometime in the future Authors: Yu, Z., Brannigan, J.A., Rangachari, K., Heal, W.P., Wilkinson, A.J., Holder, A.A., Tate, E.W.... |
No edit summary |
||
| (9 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Plasmodium vivax N-myristoyltransferase in complex with a pyridyl inhibitor (compound 22)== | |||
<StructureSection load='4ufw' size='340' side='right'caption='[[4ufw]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ufw]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_vivax Plasmodium vivax]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UFW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UFW 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]] 1.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7Y6:4-CHLORANYL-N-[2-(3-METHOXYPHENYL)ETHANIMIDOYL]-2-PIPERIDIN-4-YLOXY-BENZAMIDE'>7Y6</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NHW:2-OXOPENTADECYL-COA'>NHW</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4ufw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ufw OCA], [https://pdbe.org/4ufw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ufw RCSB], [https://www.ebi.ac.uk/pdbsum/4ufw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ufw ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A5K1A2_PLAVS A5K1A2_PLAVS] Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins (By similarity).[RuleBase:RU000586] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
N-Myristoyltransferase (NMT) represents an attractive drug target in parasitic infections such as malaria due to its genetic essentiality and amenability to inhibition by drug-like small molecules. Scaffold simplification from previously reported inhibitors containing bicyclic cores identified phenyl derivative 3, providing a versatile platform to study the effects of substitution on the scaffold, which yielded pyridyl 19. This molecule exhibited improved enzyme and cellular potency, and reduced lipophilicity compared to inhibitor 3. Further structure-based inhibitor design led to the discovery of 30, the most potent inhibitor in this series, which showed single-digit nM enzyme affinity and sub-muM anti-plasmodial activity. | |||
Discovery of pyridyl-based inhibitors of -myristoyltransferase.,Yu Z, Brannigan JA, Rangachari K, Heal WP, Wilkinson AJ, Holder AA, Leatherbarrow RJ, Tate EW Medchemcomm. 2015 Oct 8;6(10):1767-1772. Epub 2015 Aug 19. PMID:26962430<ref>PMID:26962430</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 4ufw" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Tate | [[Category: Plasmodium vivax]] | ||
[[Category: | [[Category: Brannigan JA]] | ||
[[Category: Heal WP]] | |||
[[Category: Holder AA]] | |||
[[Category: Leatherbarrow RJ]] | |||
[[Category: Rangachari K]] | |||
[[Category: Tate EW]] | |||
[[Category: Wilkinson AJ]] | |||
[[Category: Yu Z]] | |||
Latest revision as of 14:20, 9 May 2024
Plasmodium vivax N-myristoyltransferase in complex with a pyridyl inhibitor (compound 22)Plasmodium vivax N-myristoyltransferase in complex with a pyridyl inhibitor (compound 22)
Structural highlights
FunctionA5K1A2_PLAVS Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins (By similarity).[RuleBase:RU000586] Publication Abstract from PubMedN-Myristoyltransferase (NMT) represents an attractive drug target in parasitic infections such as malaria due to its genetic essentiality and amenability to inhibition by drug-like small molecules. Scaffold simplification from previously reported inhibitors containing bicyclic cores identified phenyl derivative 3, providing a versatile platform to study the effects of substitution on the scaffold, which yielded pyridyl 19. This molecule exhibited improved enzyme and cellular potency, and reduced lipophilicity compared to inhibitor 3. Further structure-based inhibitor design led to the discovery of 30, the most potent inhibitor in this series, which showed single-digit nM enzyme affinity and sub-muM anti-plasmodial activity. Discovery of pyridyl-based inhibitors of -myristoyltransferase.,Yu Z, Brannigan JA, Rangachari K, Heal WP, Wilkinson AJ, Holder AA, Leatherbarrow RJ, Tate EW Medchemcomm. 2015 Oct 8;6(10):1767-1772. Epub 2015 Aug 19. PMID:26962430[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||