1btw
From Proteopedia
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|PDB= 1btw |SIZE=350|CAPTION= <scene name='initialview01'>1btw</scene>, resolution 1.7Å | |PDB= 1btw |SIZE=350|CAPTION= <scene name='initialview01'>1btw</scene>, resolution 1.7Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=BLY:LYSINE+BORONIC+ACID'>BLY</scene>, <scene name='pdbligand=BOC:TERT-BUTYL+HYDROGEN+CARBONATE'>BOC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HPG:HYDROXYPROPYLOXY+GROUP'>HPG</scene>, <scene name='pdbligand=PDO:1,3-PROPANDIOL'>PDO</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1btw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1btw OCA], [http://www.ebi.ac.uk/pdbsum/1btw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1btw RCSB]</span> | ||
}} | }} | ||
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[[Category: Katz, B A.]] | [[Category: Katz, B A.]] | ||
[[Category: Stroud, R M.]] | [[Category: Stroud, R M.]] | ||
| - | [[Category: | + | [[Category: tripeptideboronate 1,3-propanediol monoester-inhibited]] |
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:08:10 2008'' |
Revision as of 16:08, 30 March 2008
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| , resolution 1.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Activity: | Trypsin, with EC number 3.4.21.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
EPISELECTION: NOVEL KI ~NANOMOLAR INHIBITORS OF SERINE PROTEASES SELECTED BY BINDING OR CHEMISTRY ON AN ENZYME SURFACE
Overview
A novel class of mechanism-based inhibitors of the serine proteases is developed using epitaxial selection. Tripeptide boronates esterified by an alcohol or alcohols at the boron retain the tight binding to trypsin-like enzymes associated with transition-state analogs and incorporate additional groups that can be utilized for selectivity between proteases. Formed by reaction of a series of alcohols with the inhibitor boronate oxygen(s), the most structurally compatible alcohol-derivatized inhibitors are either selected by binding to the enzyme (epitaxial selection) or assembled by epitaxial reaction on the enzyme surface. Mass spectrometry of the derivatized boronates and X-ray crystallography of the complexes identify the chemical structures and the three-dimensional interactions of inhibitors generated. This scheme also engineers novel, potent (Ki approximately 7 nM), and more specific inhibitors of individual serine proteases, by derivitizations of compounds obtained by epitaxial selection.
About this Structure
1BTW is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Episelection: novel Ki approximately nanomolar inhibitors of serine proteases selected by binding or chemistry on an enzyme surface., Katz BA, Finer-Moore J, Mortezaei R, Rich DH, Stroud RM, Biochemistry. 1995 Jul 4;34(26):8264-80. PMID:7599119
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