# MOLECULAR STRUCTURE OF THE ADENOVIRUS CAPSID

> **NIH NIH R01** · WISTAR INSTITUTE · 1988 · $248,753

## Abstract

The molecular structure of the complex capsid of adenovirus will be
investigated at high resolution by an X-ray crystallographic analysis of
its major constituent, the coat protein hexon (Mr 3 x 109,058).  A model
for the placement of the 240 hexons within the capsid, derived using
electron microscopy, will be used to orient the individual molecules.  This
approach will yield atomic coordinates for the greater part of the outer
capsid, and for 60% of the total protein in the virion.  Further
information on other structural proteins can then be related to this
framework.  The structure determination of hexon, in progress at 2.9
angstroms resolution, will complete the definition of the 967 amino acid
chain and its correlation with the chemical sequence.  A detailed molecular
model, to atomic resolution, will be derived from model-building using
computer graphics, followed by restrained least-squares structure
refinement.  The diffraction data will be extended to the resolution limit
of approximately 2.0 angstroms using the Cornell High Energy Synchrotron
Source (CHESS).  The structure of the immunologically distinct type 5
hexon, for which isomorphous crytals are at hand, will also be determined.

Comparison of the structures will reveal the basis for the immunological
differences between hexons type 2 and 5.  Extension to other types would
reveal the differentiation of the viral coat, and indicate the reason for
the variable stability of the adenovirus capsid.  Definition of the
immunologically significant sites on hexon, corresponding to the major
antigenic determinants of adenovirus, will indicate relevant peptides,
which  could provide synthetic vaccines against adenoviral infections in
both humans and domestic animals.  Purified hexon has already been shown to
confer immunity when used in place of the complete virus, the use of which
has discontinued due to its potential oncogenicity.  The investigation will
reveal the manner in which the geometry of hexon permits different chemical
bonding to occur at each of the four independent locations within the
capsid.  The detailed amino-acid side-chain interactions will indicate the
structural basis for these discrete states.  The adenovirus capsid will
serve as a model for mammalian viruses in general.  A full understanding of
adenovirus is not only of intrinsic interest, but will also indicate the
extent to which complex systems may be studied by integrating detailed
pictures of their component molecules.

## Key facts

- **NIH application ID:** 3127099
- **Project number:** 7R01AI017270-09
- **Recipient organization:** WISTAR INSTITUTE
- **SAM.gov UEI:** DW1XZMGNFBL4
- **Principal Investigator:** ROGER M BURNETT
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1988
- **Award amount:** $248,753
- **Award type:** 7
- **Project period:** 1988-08-01 → 1990-07-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3127099

## Citation

> US National Institutes of Health, RePORTER application 3127099, MOLECULAR STRUCTURE OF THE ADENOVIRUS CAPSID (7R01AI017270-09). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3127099. Licensed CC0.

---

*[NIH grants dataset](/datasets/nih-grants) · CC0 1.0*