1os0: Difference between revisions

Revision as of 06:38, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1os0.png

Template:STRUCTURE 1os0

THERMOLYSIN WITH AN ALPHA-AMINO PHOSPHINIC INHIBITORTHERMOLYSIN WITH AN ALPHA-AMINO PHOSPHINIC INHIBITOR

Template:ABSTRACT PUBMED 12832763

About this StructureAbout this Structure

1OS0 is a Single protein structure of sequence from Bacillus thermoproteolyticus. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Tue Jul 29 06:38:18 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_1os0|  PDB=1os0  |  SCENE=  }}
-'''THERMOLYSIN WITH AN ALPHA-AMINO PHOSPHINIC INHIBITOR'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12832763}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12832763 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12832763}}
 ==About this Structure==
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 [[Category: Neprylisin]]
 [[Category: Thermolysin]]
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