29 research outputs found
Structural studies on mannose-selective glycoprotein receptors using molecular modeling techniques
Glycoproteins play important roles in various cellular
events and their presence in appropriate locations in
proper active conformations is essential for many biochemical
functions. Recent evidences suggest that some glycoproteins
may require sorting receptors for efficient exit from
the endoplasmic reticulum. These receptors need the presence
of calcium or other metal ions for their native activity.
The three-dimensional structure of such a receptor,
p58/ERGIC-53, has been recently solved by x-ray crystallography,
which is a mannose-selective lectin and contains
two Ca2+ ions. Homology search in the sequence databases
indicates a large number of proteins which bear varying degrees
of homology in a wide spectrum of species with this receptor.
In this study we have systematically searched for such
genes which are potential candidates for acting as mannosemediated
glycoprotein receptors in various species as initially
inferred from their amino acid sequence homology.
Structures of a number of proteins have been predicted using
knowledge-based homology modeling, and their ability to
act as the glycoprotein receptor has been explored by examining
the nature of sugar-binding site. Tetramer of mannose
was docked in the binding pockets of the modeled structures
followed by energy minimization and molecular dynamics
to obtain most probable structures of the complexes. Properties
of these modeled complexes were studied to examine
the nature of physicochemical forces involved in the complex
formation and compared with p58/ERGIC-53-mannose complex