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American Journal of Biochemistry and Molecular Biology
  Year: 2011 | Volume: 1 | Issue: 4 | Page No.: 375-388
DOI: 10.3923/ajbmb.2011.375.388
The Mushroom Lectins Show Three Types of Conserved Domain in a Bioinformatics Analysis
Feroz Khan and M. Islam Khan

Abstract:
The primary object of this study was to find conserved domains and sequence homology in the mushroom lectins. Mushroom lectins, a group of carbohydrate binding proteins from fungi, have attracted wider attention due to their importance in the bio-medical research. Unlike plant lectins, they are much diverse in their structures, sequences and carbohydrate recognition properties. In the present study, 22 sequences of lectins and homologous putative proteins from class Agaricomycetes in fungi comprising edible as well as toxic mushrooms from NCBI protein database were collected and analyzed to understand their evolutionary homology and to find presence of conserved domains. Based on the phylogeny tree, three major groups were identified. Group-1 consists of nine proteins and is characterized by the presence of Gal-Binding lectin domain, however large sequence diversity among the members was observed. Group-2 consists of six proteins and is characterized by the presence of fungal fruit body lectin domain. Members of Group-2 showed high homology with each others as compared to Group-1 and 3. Group-3 consists of five proteins and is characterized by the presence of ricin-B like domain. In the study two lectins from Laetiporus sulphureus and Psathyrella velutina were also identified that showed huge difference in the sequence from other members and characterized by unique structures. In conclusion, based on this study, mushroom lectins were divided in to three groups on the basis of conserved domains and their mutual homology.
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How to cite this article:

Feroz Khan and M. Islam Khan, 2011. The Mushroom Lectins Show Three Types of Conserved Domain in a Bioinformatics Analysis. American Journal of Biochemistry and Molecular Biology, 1: 375-388.

DOI: 10.3923/ajbmb.2011.375.388

URL: https://scialert.net/abstract/?doi=ajbmb.2011.375.388

 
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