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Updated: May 14, 2026
12:38
Structure of HIV-1 Capsid Assemblies by Cryo-electron Microscopy and Iterative Helical Real-space Reconstruction
Published on: August 9, 2011
Viral capsid proteins are segregated in structural fold space
Shanshan Cheng1, Charles L Brooks
1Department of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, Michigan, USA.
Plos Computational Biology
|February 15, 2013
Summary
Viral capsid proteins exhibit unique structural folds, distinct from cellular proteins. This finding offers insights into viral evolution and guides the design of virus-based nanoplatforms for diverse applications.
Area of Science:
- Structural biology
- Virology
- Biophysics
Background:
- Viral capsid proteins form unique, large, symmetrical architectures.
- The jelly-roll topology is common in viral capsid proteins.
- Understanding capsid protein structural uniqueness is crucial.
Purpose of the Study:
- To determine if viral capsid proteins are structurally unique in terms of protein folds.
- To compare viral capsid protein folds with non-viral protein domains.
Main Methods:
- Structure-alignment based clustering of viral capsid proteins from VIPERdb.
- Comparison of viral capsid protein folds with SCOP database domains using Template Modeling (TM)-score.
- Statistical analysis using permutation tests to assess significance.
Main Results:
- Identified 2078 structural relatives of capsid proteins in non-capsid sets.
- Covered 210 distinct protein folds shared between viral capsid proteins and non-capsid proteins.
- Demonstrated statistically significant segregation of viral capsid proteins in structural fold space (p < 0.0001).
Conclusions:
- Viral capsid proteins are structurally segregated in fold space.
- Evolutionary constraints on capsid protein folds are linked to assembled architecture.
- Results provide a guiding principle for virus-based nanoplatform design in nanomedicine and materials science.
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