1os0
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(New page: 200px<br /><applet load="1os0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1os0, resolution 2.10Å" /> '''THERMOLYSIN WITH AN ...)
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Revision as of 21:01, 20 November 2007
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THERMOLYSIN WITH AN ALPHA-AMINO PHOSPHINIC INHIBITOR
Overview
A new alpha-aminophosphinic compound able to inhibit both zinc-containing, exopeptidases and endopeptidases has been crystallized with TLN as a model, in order to investigate the mode of zinc recognition by the phosphinic, moiety and to evaluate the potential role of the free alpha-amino group in, the formation of enzyme-inhibitor complexes. In addition to the main, interactions between the backbone of the inhibitor and the enzyme active, site, it is observed that the phosphinic group acts as a distorted, bidentate ligand for the zinc ion, while the free alpha-amino function, does not directly participate in interactions within the active site., Association of the present data and the K(i) values of various analogues, of the inhibitor towards TLN and neprilysin suggests differences in the, hydrophobicity of the S(1)-S(2) domains of the enzymes. This could be, taken into account in the design of selective inhibitors.
About this Structure
1OS0 is a Single protein structure of sequence from Bacillus thermoproteolyticus with ZN, CA, PPH and DMS as ligands. Active as Thermolysin, with EC number 3.4.24.27 Full crystallographic information is available from OCA.
Reference
Interactions of a new alpha-aminophosphinic derivative inside the active site of TLN (thermolysin): a model for zinc-metalloendopeptidase inhibition., Selkti M, Tomas A, Gaucher JF, Prange T, Fournie-Zaluski MC, Chen H, Roques BP, Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1200-5. Epub 2003, Jun 27. PMID:12832763
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