HOMOLOGY MODELING AND STRUCTURAL STUDIES OF CELL WALL BINDING PROTEIN ?-1,3, GLUCANASE FROM NEUROSPORA CRASSA
K. Ashok Kumar, S. K. Gousia, M. Mary Moses and J. Naveena Lavanya Latha*
Background: The structure of protein determines its function and its interactions with other. The regions of proteins that interact with ligands, substrates or other proteins tend to be conserved both in sequence and structure. Experimentally identifying and characterizing metal ion binding sites is a time consuming and costly process. There are many computational methods developed to identify metal ion binding sites, but most use only sequence information. Methods: The work reported here contains, the stereo chemical quality of the protein model was checked by using in silico analysis with PROCHECK and QMEAN servers. Results: In this paper the protein with 4 metal binding sites shows highest metal binding probability for the metal namely calcium in sites 1 & 3 with the metal probability of 0.627722 & 0.757665; magnesium in site 2 with the probability of 0.571190 and zinc in site 4 with the probability of 0.643216 was shown. The 85.9 % residues in the core region of Ramachandran plot showing high accuracy of protein model and the QMEAN Z-score of -3.03 indicates the overall model quality of protein. Conclusions: The result of the study may be a guiding point for further investigations on Lam G protein and metal binding sites.
Keywords: Cell Wall Proteins, ?-1,3, Glucanase, Metal Binding Sites, Homology Modeling, Neurospora Crassa.
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