4b12: Difference between revisions

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<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=4b12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b12 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b12 RCSB], [http://www.ebi.ac.uk/pdbsum/4b12 PDBsum]</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=4b12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b12 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b12 RCSB], [http://www.ebi.ac.uk/pdbsum/4b12 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
[[http://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]
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 02:55, 25 December 2014

Plasmodium vivax N-myristoyltransferase with a bound benzofuran inhibitor (compound 23)Plasmodium vivax N-myristoyltransferase with a bound benzofuran inhibitor (compound 23)

Structural highlights

4b12 is a 3 chain structure with sequence from Plasmodium vivax. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , , ,
Activity:Glycylpeptide N-tetradecanoyltransferase, with EC number 2.3.1.97
Resources:FirstGlance, OCA, RCSB, PDBsum

Function

[A5K1A2_PLAVS] Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins (By similarity).[RuleBase:RU000586]

Publication Abstract from PubMed

Design of inhibitors for N-myristoyltransferase (NMT), an enzyme responsible for protein trafficking in Plasmodium falciparum , the most lethal species of parasites that cause malaria, is described. Chemistry-driven optimization of compound 1 from a focused NMT inhibitor library led to the identification of two early lead compounds 4 and 25, which showed good enzyme and cellular potency and excellent selectivity over human NMT. These molecules provide a valuable starting point for further development.

Design and Synthesis of Inhibitors of Plasmodium falciparum N-Myristoyltransferase, A Promising Target for Antimalarial Drug Discovery.,Yu Z, Brannigan JA, Moss DK, Brzozowski AM, Wilkinson AJ, Holder AA, Tate EW, Leatherbarrow RJ J Med Chem. 2012 Oct 15. PMID:23035716[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Yu Z, Brannigan JA, Moss DK, Brzozowski AM, Wilkinson AJ, Holder AA, Tate EW, Leatherbarrow RJ. Design and Synthesis of Inhibitors of Plasmodium falciparum N-Myristoyltransferase, A Promising Target for Antimalarial Drug Discovery. J Med Chem. 2012 Oct 15. PMID:23035716 doi:http://dx.doi.org/10.1021/jm301160h

4b12, resolution 1.79Å

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