Structure of a 16-nm Cage Designed by Using Protein Oligomers

Author:

Lai Yen-Ting1,Cascio Duilio2,Yeates Todd O.23

Affiliation:

1. University of California Los Angeles (UCLA) Biomedical Engineering Interdepartmental Program, Los Angeles, CA 90095, USA.

2. UCLA–Department of Energy (DOE) Institute for Genomics and Proteomics, Los Angeles, CA 90095, USA.

3. UCLA Department of Chemistry and Biochemistry, Los Angeles, CA 90095, USA.

Abstract

Design and Build Self-assembling biomolecules are attractive building blocks in the development of functional materials. Sophisticated DNA-based materials have been developed; however, progress in designing protein-based materials has been slower. King et al. (p. 1171 ) describe a general computational method in which protein building blocks are first symmetrically docked onto a target architecture, and then binding interfaces that drive self-assembly of the building blocks are designed. As a proof of principle, trimeric building blocks were used to design self-assembling 12-subunit complexes with tetrahedral symmetry and 24-subunit complexes with octahedral symmetry. Lai et al. (p. 1129 ) were able to build a 12-subunit tetrahedral protein cage from fused oligomeric protein domains.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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