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Crystal structure of NS-134 in complex with bovine cathepsin B: a two-headed epoxysuccinyl inhibitor extends along the entire active-site cleft.

Stern I, Schaschke N, Moroder L, Turk D
Biochem J 381 511-7 (2004)
Cited: 23 times
EuropePMC logo PMID: 15084146

Abstract

The crystal structure of the inhibitor NS-134 in complex with bovine cathepsin B reveals that functional groups attached to both sides of the epoxysuccinyl reactive group bind to the part of active-site cleft as predicted. The -Leu-Pro-OH side binds to the primed binding sites interacting with the His110 and His111 residues with its C-terminal carboxy group, whereas the -Leu-Gly-Meu (-Leu-Gly-Gly-OMe) part (Meu, methoxycarbonylmethyl) binds along the non-primed binding sites. Comparison with the propeptide structures of cathepsins revealed that the binding of the latter part is least similar to the procathepsin B structure; this result, together with the two-residue shift in positioning of the Leu-Gly-Gly part, suggests that the propeptide structures of the cognate enzymes may not be the best starting point for the design of reverse binding inhibitors.

Articles - 1sp4 mentioned but not cited (4)

  1. Collagenolytic activities of the major secreted cathepsin L peptidases involved in the virulence of the helminth pathogen, Fasciola hepatica. Robinson MW, Corvo I, Jones PM, George AM, Padula MP, To J, Cancela M, Rinaldi G, Tort JF, Roche L, Dalton JP. PLoS Negl Trop Dis 5 e1012 (2011)
  2. Crystal structure of NS-134 in complex with bovine cathepsin B: a two-headed epoxysuccinyl inhibitor extends along the entire active-site cleft. Stern I, Schaschke N, Moroder L, Turk D. Biochem J 381 511-517 (2004)
  3. Foot-and-mouth disease virus leader proteinase: structural insights into the mechanism of intermolecular cleavage. Steinberger J, Grishkovskaya I, Cencic R, Juliano L, Juliano MA, Skern T. Virology 468-470 397-408 (2014)
  4. Conserved residues Arg188 and Asp302 are critical for active site organization and catalysis in human ABO(H) blood group A and B glycosyltransferases. Gagnon SML, Legg MSG, Polakowski R, Letts JA, Persson M, Lin S, Zheng RB, Rempel B, Schuman B, Haji-Ghassemi O, Borisova SN, Palcic MM, Evans SV. Glycobiology 28 624-636 (2018)


Reviews citing this publication (4)

  1. Cysteine cathepsins: from structure, function and regulation to new frontiers. Turk V, Stoka V, Vasiljeva O, Renko M, Sun T, Turk B, Turk D. Biochim Biophys Acta 1824 68-88 (2012)
  2. Chemical tools for activity-based proteomics. Hagenstein MC, Sewald N. J Biotechnol 124 56-73 (2006)
  3. (2S,3S)-Oxirane-2,3-dicarboxylic acid: a privileged platform for probing human cysteine cathepsins. Schaschke N. J Biotechnol 129 308-315 (2007)
  4. The cathepsins contribute to life and death in the placenta. Luft FC. J Mol Med (Berl) 84 259-261 (2006)

Articles citing this publication (15)

  1. Targeting Cathepsin B for Cancer Therapies. Ruan H, Hao S, Young P, Zhang H. Horiz Cancer Res 56 23-40 (2015)
  2. Design, synthesis, and evaluation of in vivo potency and selectivity of epoxysuccinyl-based inhibitors of papain-family cysteine proteases. Sadaghiani AM, Verhelst SH, Gocheva V, Hill K, Majerova E, Stinson S, Joyce JA, Bogyo M. Chem Biol 14 499-511 (2007)
  3. Novel mechanism of cathepsin B inhibition by antibiotic nitroxoline and related compounds. Mirković B, Renko M, Turk S, Sosič I, Jevnikar Z, Obermajer N, Turk D, Gobec S, Kos J. ChemMedChem 6 1351-1356 (2011)
  4. Cathepsin B is essential for regeneration of scratch-wounded normal human epidermal keratinocytes. Büth H, Luigi Buttigieg P, Ostafe R, Rehders M, Dannenmann SR, Schaschke N, Stark HJ, Boukamp P, Brix K. Eur J Cell Biol 86 747-761 (2007)
  5. Multiple cathepsin B isoforms in schistosomula of Trichobilharzia regenti: identification, characterisation and putative role in migration and nutrition. Dvorák J, Delcroix M, Rossi A, Vopálenský V, Pospísek M, Sedinová M, Mikes L, Sajid M, Sali A, McKerrow JH, Horák P, Caffrey CR. Int J Parasitol 35 895-910 (2005)
  6. Selective targeting of tumor and stromal cells by a nanocarrier system displaying lipidated cathepsin B inhibitor. Mikhaylov G, Klimpel D, Schaschke N, Mikac U, Vizovisek M, Fonovic M, Turk V, Turk B, Vasiljeva O. Angew Chem Int Ed Engl 53 10077-10081 (2014)
  7. Expression characterization and activity analysis of a cathepsin B from Pacific abalone Haliotis discus hannai. Qiu R, Liu X, Hu YH, Sun BG. Fish Shellfish Immunol 34 1376-1382 (2013)
  8. Quantitative evaluation of each catalytic subsite of cathepsin B for inhibitory activity based on inhibitory activity-binding mode relationship of epoxysuccinyl inhibitors by X-ray crystal structure analyses of complexes. Watanabe D, Yamamoto A, Tomoo K, Matsumoto K, Murata M, Kitamura K, Ishida T. J Mol Biol 362 979-993 (2006)
  9. Solid-phase synthesis of double-headed epoxysuccinyl activity-based probes for selective targeting of papain family cysteine proteases. Verhelst SH, Bogyo M. Chembiochem 6 824-827 (2005)
  10. BODIPY-Caged Photoactivated Inhibitors of Cathepsin B Flip the Light Switch on Cancer Cell Apoptosis. Toupin NP, Arora K, Shrestha P, Peterson JA, Fischer LJ, Rajagurubandara E, Podgorski I, Winter AH, Kodanko JJ. ACS Chem Biol 14 2833-2840 (2019)
  11. Foot and mouth disease leader protease (Lbpro): Investigation of prime side specificity allows the synthesis of a potent inhibitor. Nogueira Santos JA, Assis DM, Gouvea IE, Júdice WA, Izidoro MA, Juliano MA, Skern T, Juliano L. Biochimie 94 711-718 (2012)
  12. Recombinant expression, characterization and expressional analysis of clam Meretrix meretrix cathepsin B, an enzyme involved in nutrient digestion. Yao X, Zhang J, Sun J, Liu B. Mol Biol Rep 38 1861-1868 (2011)
  13. Peptidyl epoxides extended in the P' direction as cysteine protease inhibitors: effect on affinity and mechanism of inhibition. Perlman N, Hazan M, Shokhen M, Albeck A. Bioorg Med Chem 16 9032-9039 (2008)
  14. E-64c-hydrazide: a lead structure for the development of irreversible cathepsin C inhibitors. Radzey H, Rethmeier M, Klimpel D, Grundhuber M, Sommerhoff CP, Schaschke N. ChemMedChem 8 1314-1321 (2013)
  15. Inhibition of cathepsin L by epoxysuccinyl peptides simultaneously addressing active-site and remote-site regions. Schaschke N, Assfalg-Machleidt I, Machleidt W. Chembiochem 9 1721-1724 (2008)


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