ArticleMolecular biology reports2012
Structural characterization of plant defensin protein superfamily.
Article in Molecular biology reports, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 28 citations in OpenAlex.
- Insect α-Amylases and Their Application in Pest Management.Molecules (Basel, Switzerland) · 2023Review
- Article
- Protein Surface Interactions-Theoretical and Experimental Studies.Frontiers in molecular biosciences · 2021Review
- Membrane Active Peptides and Their Biophysical Characterization.Biomolecules · 2018Review
- Antimicrobial Peptides from Plants.Pharmaceuticals (Basel, Switzerland) · 2015Review
- The antifungal plant defensin AhPDF1.1b is a beneficial factor involved in adaptive response to zinc overload when it is expressed in yeast cells.MicrobiologyOpen · 2015Article
- An RNA sequencing transcriptome analysis reveals novel insights into molecular aspects of the nitrate impact on the nodule activity of Medicago truncatula.Plant physiology · 2014Article
- Are ticks venomous animals?Frontiers in zoology · 2014Article
- Evolutionary tinkering of the expression of PDF1s suggests their joint effect on zinc tolerance and the response to pathogen attack.Frontiers in plant science · 2014Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plant defensins represent a major innate immune protein superfamily with strong inhibitory effects on infectious diseases of humans, antifungal/antibacterial activities, proteinase and insect amylase inhibitory activities. They are generally defined by their conserved cysteine scaffold with α-helix and triple strand anti parallel β-sheet connected to the scaffold. With the genome of more plant species being fully sequenced, significant information about newly sequenced defensin proteins has been revealed. In this paper, we identify members of defensin protein families across plant species and use protein-modeling-based structural reconstitution to reveal specific three dimensional hidden features of plant defensins mediating defense responses and other interesting biological activities in plants. Our data revealed that plant defensins are structurally similar to their insect counterparts despite the low amino acid sequence similarity between these two organisms. The molecular and structural relationship among plant defensins and defensins from other species is discussed.
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