2bb7
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(New page: 200px<br /><applet load="2bb7" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bb7, resolution 1.700Å" /> '''Mn Form Of E. coli ...)
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Revision as of 06:34, 21 November 2007
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Mn Form Of E. coli Methionine Aminopeptidase In Complex With a quinolinyl sulfonamide inhibitor
Overview
Quinolinyl sulfonamides, such as N-(quinolin-8-yl)methanesulfonamide (10), and N-(5-chloroquinolin-8-yl)methanesulfonamide (11), were identified as, potent methionine aminopeptidase (MetAP) inhibitors by high throughput, screening of a diverse chemical library of small organic compounds. They, showed different inhibitory potencies on Co(II)-, Ni(II)-, Fe(II)-, Mn(II)-, and Zn(II)-forms of Escherichia coli MetAP, and their inhibition, is dependent on metal concentration. X-ray structures of E. coli MetAP, complexed with 10 revealed that the inhibitor forms a metal complex with, the residue H79 at the enzyme active site; the complex is further, stabilized by an extended H-bond and metal interaction network. Analysis, of the inhibition of MetAP by these inhibitors indicates that this is a, typical mechanism of inhibition for many non-peptidic MetAP inhibitors and, emphasizes the importance of defining in vitro conditions for identifying, and evaluating MetAP inhibitors that will be capable of giving information, relevant to the in vivo situation.
About this Structure
2BB7 is a Single protein structure of sequence from Escherichia coli with MN, NA and QMS as ligands. Active as Methionyl aminopeptidase, with EC number 3.4.11.18 Full crystallographic information is available from OCA.
Reference
Metal mediated inhibition of methionine aminopeptidase by quinolinyl sulfonamides., Huang M, Xie SX, Ma ZQ, Hanzlik RP, Ye QZ, Biochem Biophys Res Commun. 2006 Jan 13;339(2):506-13. Epub 2005 Nov 15. PMID:16300729
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