Scientific article
Data paper
Open access

Geometric description of self-interaction potential in symmetric protein complexes

Published inScientific data, vol. 6, no. 1
Publication date2019-05-17
First online date2019-05-17

Proteins can self-associate with copies of themselves to form symmetric complexes called homomers. Homomers are widespread in all kingdoms of life and allow for unique geometric and functional properties, as reflected in viral capsids or allostery. Once a protein forms a homomer, however, its internal symmetry can compound the effect of point mutations and trigger uncontrolled self-assembly into high-order structures. We identified mutation hot spots for supramolecular assembly, which are predictable by geometry. Here, we present a dataset of descriptors that characterize these hot spot positions both geometrically and chemically, as well as computer scripts allowing the calculation and visualization of these properties for homomers of choice. Since the biological relevance of homomers is not readily available from their X-ray crystallographic structure, we also provide reliability estimates obtained by methods we recently developed. These data have implications in the study of disease-causing mutations, protein evolution and can be exploited in the design of biomaterials.

Affiliation Not a UNIGE publication
  • Israel Science Foundation - [1452/18]
  • Israel Science Foundation (ISF) - [2179/14]
Citation (ISO format)
EMPEREUR-MOT, Charly et al. Geometric description of self-interaction potential in symmetric protein complexes. In: Scientific data, 2019, vol. 6, n° 1. doi: 10.1038/s41597-019-0058-x
Main files (1)
Article (Published version)
ISSN of the journal2052-4463

Technical informations

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