INVESTIGATION OF CONFORMATIONAL PROPERTIES OF RESIDUES NEAR 5-FOLD SYMMETRY AXI

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Human Rhinovirus (HRV), a causative agent of the common cold, is a well studied pharmaceutical target with considerable structural information known about it. Small molecule compounds bind to the HRV viral protein (VP1) in an internal pocket located near the 5-fold symmetry axis of the capsid shell, and interrupt the virus life cycle by inhibiting the uncoating process. We want to study the uncoating process and how drug effect it by simulation. Simulation study will give detail insight for new drug discovery for viruses of same family.