Comparative modelling of barley‐grain aspartic proteinase: A structural rationale for observed hydrolytic specificity
@article{Guruprasad1994ComparativeMO, title={Comparative modelling of barley‐grain aspartic proteinase: A structural rationale for observed hydrolytic specificity}, author={Kunchur Guruprasad and Kirsi Törmäkangas and Jukka Kervinen and Tom L. Blundell}, journal={FEBS Letters}, year={1994}, volume={352} }
86 Citations
Structure and possible function of aspartic proteinases in barley and other plants.
- Chemistry, MedicineAdvances in experimental medicine and biology
- 1995
The aim of this short article is to review the literature on plant aspartic proteinases in general as well as to present more detailed information on our studies on the barley aspartic proteinase.…
Structure and function of plant aspartic proteinases.
- BiologyEuropean journal of biochemistry
- 2004
New questions concerning novel structure-function relationships among plant aspartic proteinases are now starting to be addressed, and their involvement in protein processing or degradation under different conditions and in different stages of plant development suggests some functional specialization.
In Silico Insights into Protein-Protein Interactions and Folding Dynamics of the Saposin-Like Domain of Solanum tuberosum Aspartic Protease
- ChemistryPloS one
- 2014
The results indicated that the plant-specific insert may adopt a tertiary structure similar to the characteristic saposin fold and suggest a potential new structural motif among sapos in-fold proteins in the large and diverse SAPLIP family.
Aspartic proteinases: The structures and functions of a versatile superfamily of enzymes
- Biology, Chemistry
- 1995
This paper reviews the structure and function of monomeric eukaryotic aspartic proteinases and their inhibitors, including recent analyses of the sequences and the three-dimensional structural models…
Construction, expression and characterization of a chimaeric mammalian-plant aspartic proteinase.
- BiologyThe Biochemical journal
- 2003
This study highlights the use of a chimaeric enzyme strategy in order to characterize unique protein domains within enzyme families, and, for the first time, a putative structure-function role for the PSS as it pertains to plant aspartic proteinases.
Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting
- BiologyThe EMBO journal
- 1999
Structural analysis of prophytepsin led to the identification of a putative membrane receptor‐binding site involved in Golgi‐mediated transport to vacuoles, suggesting that all saposins and saposin‐like domains share a common topology.
Comparative structure-function characterization of the saposin-like domains from potato, barley, cardoon and Arabidopsis aspartic proteases.
- BiologyBiochimica et biophysica acta. Biomembranes
- 2017
Crystal Structure of Cardosin A, a Glycosylated and Arg-Gly-Asp-containing Aspartic Proteinase from the Flowers ofCynara cardunculus L.*
- Chemistry, BiologyThe Journal of Biological Chemistry
- 1999
Based on the crystal structure, a possible mechanism whereby cardosin A might be orientated at the cell surface of the style to interact with its putative receptor from pollen is proposed.
Plant aspartic proteinases: enzymes on the way to a function
- Biology
- 1999
Plant aspartic proteinases have been characterized from seeds, flowers and leaves of a number of different species and recent intriguing results suggest possible roles for these enzymes in programmed cell-death of tissues and in pathogen resistance.
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