PDB 1XR6

Christian Tyler Marcum

Medicinal Chemistry – Dr. Benjamin Clayton

The Crystal Structure of the RNA Polymerase from the Human Rhinovirus

Human rhinoviruses (Fig. 1) are the viral agents responsible for the common cold and

flu-like symptoms in humans. This structure is an x-ray crystallography of the RNA Polymerase

from the human rhinovirus accurate to 2.5 angstroms. Its polymerase function is key to the

continuation of the viral RNA and, therefore, the rhinovirus itself. As one can surmise, the

polymerase is key in the reproduction of the viral RNA (therefore the virus itself) and thus is a

target for many new anti-viral agents. Its dimensions are 88.39, 88.39, and 186.20 angstroms.

The structure of the polymerase can best be described as a hollow ring of alpha-helixes

toward the back of the molecule, with a concurrent ring of beta-pleated sheets toward the

forefront (Fig 2.). The molecule constitutes seventeen alpha helixes of varying sizes as well as

nine beta-pleated sheets arranged all but once in anti-parallel fashion stacked against one

another. The active site is most likely the hollow section in the middle by which it can bind to the

RNA strands, though it is also suggested that anti-viral agents are likely to look for an alternative

binding site as to avoid mimicking RNA. My suggestion for an alternative binding site would be

at (Fig. 3, Site B). It happens to contain convenient binding groups as well as a nearby source for

Van der Wall’s interactions in the form of a ring.

PDB 1XR6

Figure 1.

Figure 2.

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Site B

Figure 3.