1xuj: Difference between revisions

Revision as of 16:10, 28 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:1xuj.png

Template:STRUCTURE 1xuj

TRYPSIN-KETO-BABIM-ZN+2, PH 8.2TRYPSIN-KETO-BABIM-ZN+2, PH 8.2

Template:ABSTRACT PUBMED 9468142

About this StructureAbout this Structure

1XUJ is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Design of potent selective zinc-mediated serine protease inhibitors., Katz BA, Clark JM, Finer-Moore JS, Jenkins TE, Johnson CR, Ross MJ, Luong C, Moore WR, Stroud RM, Nature. 1998 Feb 5;391(6667):608-12. PMID:9468142

Page seeded by OCA on Mon Jul 28 16:10:05 2008

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

OCA

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-'''TRYPSIN-KETO-BABIM-ZN+2, PH 8.2'''
+===TRYPSIN-KETO-BABIM-ZN+2, PH 8.2===
-==Overview==
+<!--
-Many serine proteases are targets for therapeutic intervention because they often play key roles in disease. Small molecule inhibitors of serine proteases with high affinity are especially interesting as they could be used as scaffolds from which to develop drugs selective for protease targets. One such inhibitor is bis(5-amidino-2-benzimidazolyl)methane (BABIM), standing out as the best inhibitor of trypsin (by a factor of over 100) in a series of over 60 relatively closely related analogues. By probing the structural basis of inhibition, we discovered, using crystallographic methods, a new mode of high-affinity binding in which a Zn2+ ion is tetrahedrally coordinated between two chelating nitrogens of BABIM and two active site residues, His57 and Ser 195. Zn2+, at subphysiological levels, enhances inhibition by over 10(3)-fold. The distinct Zn2+ coordination geometry implies a strong dependence of affinity on substituents. This unique structural paradigm has enabled development of potent, highly selective, Zn2+-dependent inhibitors of several therapeutically important serine proteases, using a physiologically ubiquitous metal ion.
+The line below this paragraph, {{ABSTRACT_PUBMED_9468142}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9468142 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9468142}}
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 [[Category: Designed small molecule ligand with micromolar affinity]]
 [[Category: Trypsin-sulfate-small molecule ligand]]
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