2ea2

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{{STRUCTURE_2ea2| PDB=2ea2 | SCENE= }}
{{STRUCTURE_2ea2| PDB=2ea2 | SCENE= }}
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'''h-MetAP2 complexed with A773812'''
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===h-MetAP2 complexed with A773812===
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==Overview==
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A series of aryl sulfonamides of 5,6-disubstituted anthranilic acids were identified as potent inhibitors of methionine aminopeptidase-2 (MetAP2). Small alkyl groups and 3-furyl were tolerated at the 5-position of anthranilic acid, while -OCH(3), CH(3), and Cl were found optimal for the 6-position. Placement of 2-aminoethoxy group at the 6-position enabled interaction with the second Mn(2+) but did not result in enhancement in potency. Introduction of a tertiary amino moiety at the ortho-position of the sulfonyl phenyl ring gave reduced protein binding and improved cellular activity, but led to lower oral bioavailability.
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{{ABSTRACT_PUBMED_17350258}}
==About this Structure==
==About this Structure==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Protein-ligand complex]]
[[Category: Protein-ligand complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:05:58 2008''

Revision as of 11:06, 28 July 2008

Image:2ea2.png

Template:STRUCTURE 2ea2

h-MetAP2 complexed with A773812

Template:ABSTRACT PUBMED 17350258

About this Structure

2EA2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Lead optimization of methionine aminopeptidase-2 (MetAP2) inhibitors containing sulfonamides of 5,6-disubstituted anthranilic acids., Wang GT, Mantei RA, Kawai M, Tedrow JS, Barnes DM, Wang J, Zhang Q, Lou P, Garcia LA, Bouska J, Yates M, Park C, Judge RA, Lesniewski R, Sheppard GS, Bell RL, Bioorg Med Chem Lett. 2007 May 15;17(10):2817-22. Epub 2007 Feb 25. PMID:17350258

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