ABSTRACT
Gamma secretase enzyme is a multi-subunit proteinase complex, an integral membrane protein that severs single-pass transmembrane proteins at residues intervals the transmembrane domain. The most substrates of γ- secretase are amyloid precursor protein (APP), an outsized integral membrane macromolecule that, once cleaved by each γ-and β-secretase, produces 39-42 amino acid amide known as amyloid beta whose abnormally folded fibrillar type is that the primary part of amyloid plaques found in the brains of Alzheimer's disease (AD) patients.
The gamma-secretase complex consists of 4 individual proteins: presenilin, PEN-2 (presenilin enhancer 2), APH-1 (anterior pharynx-defective 1), nicastrin. We know the structure of 2 subunits presenilin and
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Figure.12: The complex structure of all the subunits of gamma-secretase .
The Ramachandran plot analysis of the gamma protein structure is finished for the favoured region, allowed region and also the outlier regions.
The tertiary structure of the gamma-secretase is being predicted with generally number of residues in the favoured region in Ramachandran plot. The residue in favoured region and also the allowed regions are found to be 91.40 % and 6.0 % of the total residues respectively. This show good interaction of subunit structures to form the complex structure of γ-secretase.
Docked result of all the subunits
(1044residues) Number of Residue Percentage of the total
Favoured Region 954 91.4
Allowed Region 63 6.0
Outlier Region 27 2.6
Table.6: Ramachadran plot analysis of the tertiary structure generated using all the subunits of the gamma-secretase Figure.13: Ramachandran plot of the tertiary structure generated from all the subunits of gamma-secretase.
DISCUSSION AND FUTURE PERSPECTIVE
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