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}
}
Structure and possible function of aspartic proteinases in barley and other plants.
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.
TLDR
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
TLDR
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
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.
TLDR
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
TLDR
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.
Crystal Structure of Cardosin A, a Glycosylated and Arg-Gly-Asp-containing Aspartic Proteinase from the Flowers ofCynara cardunculus L.*
TLDR
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
TLDR
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.
Aspartic proteinases in Antarctic fish.
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TLDR
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It was demonstrated that altering Met287 of human cathepsin D to more polar amino acids produced active mutant enzymes with significantly altered substrate specificity.
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TLDR
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