Due to insufficiency in appropriate hepatitis E virus (HEV)
in vitro cell culture systems, our knowledge of its pathogenesis is
inadequately understood. Viral proteins entail disordered regions that are
linked with the infectivity and pathogenicity of the virus. Despite the general
belief that unique biological functions of proteins require unique 3D
structures (which dominated protein science for more than a century),
structure-less intrinsically disordered proteins (IDPs)/intrinsically
disordered protein regions (IDPRs) are functional, being able to engage in
biological activities and perform impossible tricks that are highly unlikely
for ordered proteins. The distribution of intrinsically disordered regions
(IDRs) in the ORF4 protein is of great importance in the regulation of HEV.
Thus, we examined the unstructured regions (IDRs) of this additional reading
frame encoded protein ORF4, completely embedded inside ORF1, by analysing its
IDRs, by exploiting computational methodologies. Our findings suggested that
ORF4 had the prevalence of disordered regions. IDPRs are characterized by
remarkable conformational flexibility and structural plasticity resulting in
their engagement in several biological processes. In this chapter, some wonders
of intrinsic disorder contribution to ORF4’s functions have been discussed.
Author(s) Details
Zoya Shafat
Centre for Interdisciplinary Research in Basic Sciences,
Jamia Millia Islamia, New Delhi 110025, India.
Please see the link:- https://doi.org/10.9734/bpi/mono/978-81-976007-3-9/CH3
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