4cae: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4cae|  PDB=4cae  |  SCENE=  }}
===Plasmodium vivax N-myristoyltransferase in complex with a benzothiophene inhibitor (compound 20b)===
{{ABSTRACT_PUBMED_24641010}}


The entry 4cae is ON HOLD  until Paper Publication
==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]


Authors: Rackham, M.D., Brannigan, J.A., Rangachari, K., Wilkinson, A.J., Holder, A.A., Tate, E.W., Leatherbarrow, R.J.
==About this Structure==
[[4cae]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CAE OCA].  


Description: Plasmodium vivax N-myristoyltransferase in complex with a benzothiophene inhibitor (compound 20b)
==Reference==
<ref group="xtra">PMID:024641010</ref><references group="xtra"/><references/>
[[Category: Glycylpeptide N-tetradecanoyltransferase]]
[[Category: Brannigan, J A.]]
[[Category: Holder, A A.]]
[[Category: Leatherbarrow, R J.]]
[[Category: Rackham, M D.]]
[[Category: Rangachari, K.]]
[[Category: Tate, E W.]]
[[Category: Wilkinson, A J.]]
[[Category: Benzothiophene]]
[[Category: Inhibitor]]
[[Category: Malaria]]
[[Category: Myristoylation]]
[[Category: Transferase]]

Revision as of 09:12, 2 April 2014

Template:STRUCTURE 4cae

Plasmodium vivax N-myristoyltransferase in complex with a benzothiophene inhibitor (compound 20b)

Template:ABSTRACT PUBMED 24641010

Function

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

About this Structure

4cae is a 3 chain structure. Full crystallographic information is available from OCA.

Reference

  1. Rackham MD, Brannigan JA, Rangachari K, Meister S, Wilkinson AJ, Holder AA, Leatherbarrow RJ, Tate EW. Design and Synthesis of High Affinity Inhibitors of Plasmodium falciparum and Plasmodium vivax N-Myristoyltransferases Directed by Ligand Efficiency Dependent Lipophilicity (LELP). J Med Chem. 2014 Mar 27;57(6):2773-88. doi: 10.1021/jm500066b. Epub 2014 Mar 18. PMID:24641010 doi:https://dx.doi.org/10.1021/jm500066b

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