Journal
JOURNAL OF MOLECULAR MODELING
Volume 12, Issue 2, Pages 237-248Publisher
SPRINGER
DOI: 10.1007/s00894-005-0025-7
Keywords
protein structure prediction; computational methods; TIM barrel; glycosidase
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The three-dimensional (3D) structure of the catalytic domain of Gas1p, a protein belonging to the only family of beta-(1,3)-glucan transferases so far identified in yeasts and some pathogenic fungi (family GH-72), has been predicted by combining results derived from threading methods, multiple sequence alignments and secondary-structure predictions. The 3D model has allowed the identification of several residues that are predicted to play a crucial role in structural integrity, substrate recognition and catalysis. In particular, the model of the catalytic domain can be useful for designing site-directed mutagenesis experiments and for developing inhibitors of Gas1p enzymatic activity.
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