Structural characterization of plant defensin protein superfamily |
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Authors: | Emma W Gachomo Jose C Jimenez-Lopez Adéchola Pierre Polycarpe Kayodé Lamine Baba-Moussa Simeon O Kotchoni |
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Institution: | 1.Department of Biology,Rutgers University,Camden,USA;2.Center for computational and Integrative Biology,Rutgers University,Camden,USA;3.Department of Biochemistry, Cell and Molecular Biology of Plants, Estacion Experimental del Zaidin,High Council for Scientific Research (CSIC),Granada,Spain;4.Département de Nutrition et Sciences Alimentaire,Faculté des Sciences Agronomiques Université d’Abomey-Calavi,Cotonou,Benin;5.Laboratoire de Biologie et de Typage Moléculaire en Microbiologie; Faculté des Sciences et Techniques, Université d’Abomey-Calavi,Cotonou,Benin |
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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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