2ggc: Difference between revisions

Revision as of 18:31, 21 February 2008

Novel bacterial methionine aminopeptidase inhibitors

OverviewOverview

In this article we describe the application of structural biology methods to the discovery of novel potent inhibitors of methionine aminopeptidases. These enzymes are employed by the cells to cleave the N-terminal methionine from nascent peptides and proteins. As this is one of the critical steps in protein maturation, it is very likely that inhibitors of these enzymes may prove useful as novel antibacterial agents. Involvement of crystallography at the very early stages of the inhibitor design process resulted in serendipitous discovery of a new inhibitor class, the pyrazole-diamines. Atomic-resolution structures of several inhibitors bound to the enzyme illuminate a new mode of inhibitor binding.

About this StructureAbout this Structure

2GGC is a Single protein structure of sequence from Escherichia coli with , and as ligands. Active as Methionyl aminopeptidase, with EC number 3.4.11.18 Full crystallographic information is available from OCA.

ReferenceReference

Serendipitous discovery of novel bacterial methionine aminopeptidase inhibitors., Evdokimov AG, Pokross M, Walter RL, Mekel M, Barnett BL, Amburgey J, Seibel WL, Soper SJ, Djung JF, Fairweather N, Diven C, Rastogi V, Grinius L, Klanke C, Siehnel R, Twinem T, Andrews R, Curnow A, Proteins. 2007 Feb 15;66(3):538-46. PMID:17120228

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 ==Overview==
-In this article we describe the application of structural biology methods, to the discovery of novel potent inhibitors of methionine aminopeptidases., These enzymes are employed by the cells to cleave the N-terminal, methionine from nascent peptides and proteins. As this is one of the, critical steps in protein maturation, it is very likely that inhibitors of, these enzymes may prove useful as novel antibacterial agents. Involvement, of crystallography at the very early stages of the inhibitor design, process resulted in serendipitous discovery of a new inhibitor class, the, pyrazole-diamines. Atomic-resolution structures of several inhibitors, bound to the enzyme illuminate a new mode of inhibitor binding.
+In this article we describe the application of structural biology methods to the discovery of novel potent inhibitors of methionine aminopeptidases. These enzymes are employed by the cells to cleave the N-terminal methionine from nascent peptides and proteins. As this is one of the critical steps in protein maturation, it is very likely that inhibitors of these enzymes may prove useful as novel antibacterial agents. Involvement of crystallography at the very early stages of the inhibitor design process resulted in serendipitous discovery of a new inhibitor class, the pyrazole-diamines. Atomic-resolution structures of several inhibitors bound to the enzyme illuminate a new mode of inhibitor binding.
 ==About this Structure==
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 [[Category: Methionyl aminopeptidase]]
 [[Category: Single protein]]
-[[Category: Evdokimov, A.G.]]
+[[Category: Evdokimov, A G.]]
 [[Category: Mekel, M.]]
-[[Category: Pokross, M.E.]]
+[[Category: Pokross, M E.]]
-[[Category: Walter, R.L.]]
+[[Category: Walter, R L.]]
 [[Category: CO]]
 [[Category: MET]]
@@ Line 26: / Line 26: @@
 [[Category: pita-bread fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:30:28 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:31:24 2008''