Kunitz-type soybean trypsin inhibitor revisited: refined structure of its complex with porcine trypsin reveals an insight into the interaction between a homologous inhibitor from Erythrina caffra and tissue-type plasminogen activator

Song, Hyun Kyu; Suh, Se Won

doi:10.1006/jmbi.1997.1469

Cited by 229 publications

(180 citation statements)

References 51 publications

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“…According to Boex-Fontvieille et al (16), AtWSCP most closely resembles soybean Kunitz-type trypsin inhibitor and tamarind Kunitz inhibitor, with an α-turn and 10 antiparallel β-strands forming a barrel-like structure (SI Appendix, Fig. S8) (34,35). According to studies on oryzacystatin-I and papain-like proteases, as well as on tamarind Kunitz inhibitor and its interactions with factor Xa and trypsin (34,35), we proposed an AtWSCP::RD21 interaction model (16) that was validated here.…”

Section: Discussionmentioning

confidence: 98%

Serpin1 and WSCP differentially regulate the activity of the cysteine protease RD21 during plant development in Arabidopsis thaliana

Rustgi

Boex-Fontvieille

Reinbothe

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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Proteolytic enzymes (proteases) participate in a vast range of physiological processes, ranging from nutrient digestion to blood coagulation, thrombosis, and beyond. In plants, proteases are implicated in host recognition and pathogen infection, induced defense (immunity), and the deterrence of insect pests. Because proteases irreversibly cleave peptide bonds of protein substrates, their activity must be tightly controlled in time and space. Here, we report an example of how nature evolved alternative mechanisms to fine-tune the activity of a cysteine protease dubbed RD21 (RESPONSIVE TO DESICCATION-21). One mechanism in the model plant Arabidopsis thaliana studied here comprises irreversible inhibition of RD21's activity by Serpin1, whereas the other mechanism is a result of the reversible inhibition of RD21 activity by a Kunitz protease inhibitor named water-soluble chlorophyll-binding protein (WSCP). Activity profiling, complex isolation, and homology modeling data revealed unique interactions of RD21 with Serpin1 and WSCP, respectively. Expression studies identified only partial overlaps in Serpin1 and WSCP accumulation that explain how RD21 contributes to the innate immunity of mature plants and arthropod deterrence of seedlings undergoing skotomorphogenesis and greening.protease | protease inhibitor | WSCP | Serpin1 | RD21

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Section: Discussionmentioning

confidence: 98%

Serpin1 and WSCP differentially regulate the activity of the cysteine protease RD21 during plant development in Arabidopsis thaliana

Rustgi

Boex-Fontvieille

Reinbothe

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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“…The best-known example of a serine protease in a complex with a canonical inhibitor is trypsin in a complex with the STI, where the Arg residue fi lls the hydrophobic and negatively charged S1-binding site (Figure 3 A) Song and Suh , 1998 ). The S1-binding site is the major determinant of specifi city.…”

Section: Inhibition Of the S1 Family Serine Proteasesmentioning

confidence: 99%

“…The canonical conformation of the reactive loop is stabilized in a number of ways: by hydrogen bonds, disulfi de bonds, or hydrophobic interactions, which can involve residues either from the reactive loop or scaffold residues (Song and Suh , 1998 ;Ravichandran et al , 1999 ). Radisky et al (2003Radisky et al ( , 2004Radisky et al ( , 2005 showed that the residues Arg65 and Arg67, located in the core of the chymotrypsin inhibitor 2 of the potato inhibitor 1 family, act as a spacer and that mutations of these arginines or their interacting partners disrupt the canonical conformation, resulting in the increased hydrolysis of the scissile bond.…”

Section: Inhibition Of the S1 Family Serine Proteasesmentioning

confidence: 99%

“…In another case, cospin (PIC), the Asn residue is replaced by two long residues, which Brought to you by | MIT Libraries Authenticated Download Date | 5/11/18 10:31 AM Table 2 Overview of β -trefoil protease inhibitors with an emphasis on the reactive loop involved in inhibition of S1 family proteases. Asn14 Kunitz , 1947b ;Sweet et al , 1974 ;De Meester et al , 1998 ;Song and Suh , 1998 WCI 1EYL, 4WBC, 2QYI S1 β 4- Kortt , 1980 ;Ravichandran et al , 1999Ravichandran et al , , 2001 Inhibitor from E. caffra support the canonical conformation of the reactive loop like arginines in the case of the chymotrypsin inhibitor 2 of the potato inhibitor 1 family (Radisky et al , 2003(Radisky et al , , 2004(Radisky et al , , 2005. Furthermore, the Lys at the P5 ′ position is oriented away from the protein core and makes three hydrogen bonds with the main-and side-chain atoms of the Ser residue at P1 ′ and the main-chain atoms of the Leu at P3 ′ , respectively.…”

Section: Inhibition Of the S1 Family Serine Proteasesmentioning

confidence: 99%

“…Whereas type I inhibitors, such as the bovine pancreas trypsin inhibitor (BPTI), are relatively small, composed of 50-60 residues, type II inhibitors, such as the soybean trypsin inhibitor (STI), are larger, composed of 150-200 residues. The structure of the STI in a complex with trypsin was originally determined by Sweet et al (1974) and later with an improved resolution by Song and Suh (1998) . The BPTI was extensively investigated by Huber and colleagues (Ruhlmann et al , 1973 ;Huber et al , 1974Huber et al , , 1975Walter et al , 1982 ;Bode et al , 1984 ;Wlodawer et al , 1984 ;Burgering et al , 1997 ).…”

Section: Introductionmentioning

confidence: 99%

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β-Trefoil inhibitors – from the work of Kunitz onward

Renko

Sabotič²,

Turk³

2012

Biological Chemistry

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Protein protease inhibitors are the tools of nature in controlling proteolytic enzymes. They come in different shapes and sizes. The β -trefoil protease inhibitors that come from plants, fi rst discovered by Kunitz, were later complemented with representatives from higher fungi. They inhibit serine (families S1 and S8) and cysteine proteases (families C1 and C13) as well as other hydrolases. Their versatility is the result of the plasticity of the loops coming out of the stable β -trefoil scaffold. For this reason, they display several different mechanisms of inhibition involving different positions of the loops and their combinations. Natural diversity, as well as the initial successes in de novo protein engineering, makes the β -trefoil proteins a promising starting point for the generation of strong, specifi c, multitarget inhibitors capable of inhibiting multiple types of hydrolytic enzymes and simultaneously interacting with different protein, carbohydrate, or DNA molecules. This pool of knowledge opens up new possibilities for the exploration of their naturally occurring as well as modifi ed properties for applications in many fi elds of medicine, biotechnology, and agriculture.

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Refined crystal structure (2.3 �) of a double-headed winged bean ?-chymotrypsin inhibitor and location of its second reactive site

et al. 1999

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The crystal structure of a doubleheaded ␣-chymotrypsin inhibitor, WCI, from winged bean seeds has now been refined at 2.3 Å resolution to an R-factor of 18.7% for 9,897 reflections. The crystals belong to the hexagonal space group P6 1 22 with cell parameters a ‫؍‬ b ‫؍‬ 61.8 Å and c ‫؍‬ 212.8 Å .The final model has a good stereochemistry and a root mean square deviation of 0.011 Å and 1.14°from ideality for bond length and bond angles, respectively. A total of 109 ordered solvent molecules were localized in the structure. This improved structure at 2.3 Å led to an understanding of the mechanism of inhibition of the protein against ␣-chymotrypsin. An analysis of this higher resolution structure also helped us to predict the location of the second reactive site of the protein, about which no previous biochemical information was available. The inhibitor structure is spherical and has twelve antiparallel ␤-strands with connecting loops arranged in a characteristic ␤-trefoil fold common to other homologous serine protease inhibitors in the Kunitz (STI) family as well as to some non homologous functionally unrelated proteins. A wide variation in the surface loop regions is seen in the latter ones. Proteins 1999;35:321-331.1999 Wiley-Liss, Inc.

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Kunitz-type soybean trypsin inhibitor revisited: refined structure of its complex with porcine trypsin reveals an insight into the interaction between a homologous inhibitor from Erythrina caffra and tissue-type plasminogen activator

Cited by 229 publications

References 51 publications

Serpin1 and WSCP differentially regulate the activity of the cysteine protease RD21 during plant development in Arabidopsis thaliana

Serpin1 and WSCP differentially regulate the activity of the cysteine protease RD21 during plant development in Arabidopsis thaliana

β-Trefoil inhibitors – from the work of Kunitz onward

Refined crystal structure (2.3 �) of a double-headed winged bean ?-chymotrypsin inhibitor and location of its second reactive site

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