EUROPEAN JOURNAL OF
PHARMACEUTICAL AND MEDICAL RESEARCH

( An ISO 9001:2015 Certified International Journal )

An International Peer Reviewed Journal for Pharmaceutical, Medical & Biological Sciences

An Official Publication of Society for Advance Healthcare Research (Reg. No. : 01/01/01/31674/16)

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 ISSN 2394-3211

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Abstract

HOMOLOGY MODELING AND STRUCTURAL STUDIES OF CWP- FMN-REDUCTASE FROM NEUROSPORA CRASSA

S. K. Gousia, B. Janakiram, G. Srinivas and J. Naveena Lavanya Latha*

ABSTRACT

Background: Cell wall encompasses the cells of all fungi. Walls are composites of an assortment of parts. Commonly, the wall contains fibrillar materials bound together by sugars, proteins, lipids and an assortment of polysaccharides. While the fibrillar material of the cell wall is to great extent inactive, the structure of the cell wall changes with time. The practical segments are vital in supplement transport, digestion system of non-porous substrates, correspondence, and cell wall alterations. Methods: The stereo chemical quality of the protein model was checked by using insilico analysis with PROCHECK and QMEAN servers. The metal binding sites were determined by CHED. Results: In this paper the protein with 4 metal binding sites shows highest metal binding probability for the metal namely calcium in sites 1, 2 & 3 with the metal probability of 0.398702, 0.627722 and 0.627722; magnesium in site 4 with the probability of 0.571190 were showed. The 97.8%residue in the core region of Ramachandran plot showing high accuracy of protein model and the QMEAN Z-score of -2.69 indicates the overall model quality of protein. Conclusions: The result of the study may be a guiding point for further investigations on Flavo protein and metal binding sites.

Keywords: Flavo Protein, Cell Binding Protein, Neurospora Crassa, Homology Modeling, Metal Binding Sites.


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