Literature DB >> 10708867

What can the structures of enzyme-inhibitor complexes tell us about the structures of enzyme substrate complexes?

M Laskowski1, M A Qasim.   

Abstract

Proteinases perform many beneficial functions that are essential to life, but they are also dangerous and must be controlled. Here we focus on one of the control mechanisms: the ubiquitous presence of protein proteinase inhibitors. We deal only with a subset of these: the standard mechanism, canonical protein inhibitors of serine proteinases. Each of the inhibitory domains of such inhibitors has one reactive site peptide bond, which serves all the cognate enzymes as a substrate. The reactive site peptide bond is in a combining loop which has an identical conformation in all inhibitors and in all enzyme-inhibitor complexes. There are at least 18 families of such inhibitors. They all share the conformation of the combining loops but each has its own global three-dimensional structure. Many three-dimensional structures of enzyme-inhibitor complexes were determined. They are frequently used to predict the conformation of substrates in very short-lived enzyme-substrate transition state complexes. Turkey ovomucoid third domain and eglin c have a Leu residue at P(1). In complexes with chymotrypsin, these P(1) Leu residues assume the same conformation. The relative free energies of binding of P(1) Leu (relative to either P(1) Gly or P(1) Ala) are within experimental error, the same for complexes of turkey ovomucoid third domain, eglin c, P(1) Leu variant of bovine pancreatic trypsin inhibitor and of a substrate with chymotrypsin. Therefore, the P(1) Leu conformation in transition state complexes is predictable. In contrast, the conformation of P(1) Lys(+) is strikingly different in the complexes of Lys(18) turkey ovomucoid third domain and of bovine pancreatic trypsin inhibitor with chymotrypsin. The relative free energies of binding are also quite different. Yet, the relative free energies of binding are nearly identical for Lys(+) in turkey ovomucoid third domain and in a substrate, thus allowing us to know the structure of the latter. Similar reasoning is applied to a few other systems.

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Year:  2000        PMID: 10708867     DOI: 10.1016/s0167-4838(99)00284-8

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  66 in total

1.  PLANT-PIs: a database for plant protease inhibitors and their genes.

Authors:  F De Leo; M Volpicella; F Licciulli; S Liuni; R Gallerani; L R Ceci
Journal:  Nucleic Acids Res       Date:  2002-01-01       Impact factor: 16.971

2.  Purification, crystallization and X-ray characterization of a Kunitz-type trypsin inhibitor protein from the seeds of chickpea (Cicer arietinum).

Authors:  Urvashi Sharma; C G Suresh
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2011-05-26

3.  Structural basis of trypsin inhibition and entomotoxicity of cospin, serine protease inhibitor involved in defense of Coprinopsis cinerea fruiting bodies.

Authors:  Jerica Sabotič; Silvia Bleuler-Martinez; Miha Renko; Petra Avanzo Caglič; Sandra Kallert; Borut Štrukelj; Dušan Turk; Markus Aebi; Janko Kos; Markus Künzler
Journal:  J Biol Chem       Date:  2011-12-13       Impact factor: 5.157

Review 4.  Evolutionary families of peptidase inhibitors.

Authors:  Neil D Rawlings; Dominic P Tolle; Alan J Barrett
Journal:  Biochem J       Date:  2004-03-15       Impact factor: 3.857

5.  A clogged gutter mechanism for protease inhibitors.

Authors:  Evette S Radisky; Daniel E Koshland
Journal:  Proc Natl Acad Sci U S A       Date:  2002-07-25       Impact factor: 11.205

6.  Molecular characterization of Ancylostoma ceylanicum Kunitz-type serine protease inhibitor: evidence for a role in hookworm-associated growth delay.

Authors:  Daniel Chu; Richard D Bungiro; Maureen Ibanez; Lisa M Harrison; Eva Campodonico; Brian F Jones; Juliusz Mieszczanek; Petr Kuzmic; Michael Cappello
Journal:  Infect Immun       Date:  2004-04       Impact factor: 3.441

7.  pH dependence thermal stability of a chymotrypsin inhibitor from Schizolobium parahyba seeds.

Authors:  Rozeni C L Teles; Leonardo de A Calderon; Francisco J Medrano; João A R G Barbosa; Beatriz G Guimarães; Marcelo M Santoro; Sonia M de Freitas
Journal:  Biophys J       Date:  2005-03-11       Impact factor: 4.033

Review 8.  The many faces of protease-protein inhibitor interaction.

Authors:  Jacek Otlewski; Filip Jelen; Malgorzata Zakrzewska; Arkadiusz Oleksy
Journal:  EMBO J       Date:  2005-03-03       Impact factor: 11.598

9.  Crystal structure of the Bowman-Birk Inhibitor from Vigna unguiculata seeds in complex with beta-trypsin at 1.55 A resolution and its structural properties in association with proteinases.

Authors:  João Alexandre R G Barbosa; Luciano P Silva; Rozeni C L Teles; Gisele F Esteves; Ricardo B Azevedo; Manuel M Ventura; Sonia M de Freitas
Journal:  Biophys J       Date:  2006-12-01       Impact factor: 4.033

10.  The trypsin inhibitor panulirin regulates the prophenoloxidase-activating system in the spiny lobster Panulirus argus.

Authors:  Rolando Perdomo-Morales; Vivian Montero-Alejo; Gerardo Corzo; Vladimir Besada; Yamile Vega-Hurtado; Yamile González-González; Erick Perera; Marlene Porto-Verdecia
Journal:  J Biol Chem       Date:  2013-09-18       Impact factor: 5.157

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