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X-ray and spectrophotometric studies of the binding of proflavin to the S1 specificity pocket of human alpha-thrombin.

Conti E, Rivetti C, Wonacott A, Brick P
FEBS Lett 425 229-33 (1998)
Cited: 13 times
EuropePMC logo PMID: 9559654

Abstract

Proflavin can be used to study the interactions of inhibitors and substrates with thrombin by monitoring the changes in the visible absorption spectrum that occur on dye displacement. We have used microspectrophotometric methods to investigate the binding of proflavin to crystals of an alpha-thrombin-hirugen complex and have determined the structure by X-ray crystallography. The proflavin molecule binds in the S1 pocket of the enzyme with one of the amino groups hydrogen bonded to the carboxylate of Asp-189 while the protonated ring nitrogen is hydrogen bonded to the carbonyl of Gly-219. This result indicates that the proflavin displacement assay can be used to specifically monitor the binding of inhibitors to the S1 pocket.

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Reviews citing this publication (1)

  1. Natural occurring polyphenols as template for drug design. Focus on serine proteases. Cuccioloni M, Mozzicafreddo M, Bonfili L, Cecarini V, Eleuteri AM, Angeletti M. Chem Biol Drug Des 74 1-15 (2009)

Articles citing this publication (9)

  1. Low dielectric response in enzyme active site. Mertz EL, Krishtalik LI. Proc Natl Acad Sci U S A 97 2081-2086 (2000)
  2. A comparison of the pharmacophore identification programs: Catalyst, DISCO and GASP. Patel Y, Gillet VJ, Bravi G, Leach AR. J Comput Aided Mol Des 16 653-681 (2002)
  3. Fragment screening: an introduction. Leach AR, Hann MM, Burrows JN, Griffen EJ. Mol Biosyst 2 430-446 (2006)
  4. Flavonoids inhibit the amidolytic activity of human thrombin. Mozzicafreddo M, Cuccioloni M, Eleuteri AM, Fioretti E, Angeletti M. Biochimie 88 1297-1306 (2006)
  5. Fragment screening by biochemical assay. Barker J, Courtney S, Hesterkamp T, Ullmann D, Whittaker M. Expert Opin Drug Discov 1 225-236 (2006)
  6. Measurement of Ligand-Target Residence Times by 1H Relaxation Dispersion NMR Spectroscopy. Moschen T, Grutsch S, Juen MA, Wunderlich CH, Kreutz C, Tollinger M. J Med Chem 59 10788-10793 (2016)
  7. Aflatoxin B1 misregulates the activity of serine proteases: possible implications in the toxicity of some mycotoxin. Cuccioloni M, Mozzicafreddo M, Barocci S, Ciuti F, Re L, Eleuteri AM, Angeletti M. Toxicol In Vitro 23 393-399 (2009)
  8. Binding of alkaloids into the S1 specificity pocket of α-chymotrypsin: evidence from induced circular dichroism spectra. Zsila F, Kámán J, Bogányi B, Józsvai D. Org Biomol Chem 9 4127-4137 (2011)
  9. Protonation linked equilibria and apparent affinity constants: the thermodynamic profile of the alpha-chymotrypsin-proflavin interaction. Bruylants G, Wintjens R, Looze Y, Redfield C, Bartik K. Eur Biophys J 37 11-18 (2007)


Related citations provided by authors (1)

  1. Structure of the Hirugen and Hirulog 1 Complexes of Alpha-Thrombin. Skrzypczak-Jankun E, Carperos VE, Ravichandran KG, Tulinsky A, Westbrook M, Maraganore JM J. Mol. Biol. 221 1379- (1991)

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