EXCESP: A Structure-Based Online Database for Extracellular Interactome of Cell Surface Proteins in Humans

J Proteome Res. 2022 Feb 4;21(2):349-359. doi: 10.1021/acs.jproteome.1c00612. Epub 2022 Jan 3.

Abstract

The interactions between ectodomains of cell surface proteins are vital players in many important cellular processes, such as regulating immune responses, coordinating cell differentiation, and shaping neural plasticity. However, while the construction of a large-scale protein interactome has been greatly facilitated by the development of high-throughput experimental techniques, little progress has been made to support the discovery of extracellular interactome for cell surface proteins. Harnessed by the recent advances in computational modeling of protein-protein interactions, here we present a structure-based online database for the extracellular interactome of cell surface proteins in humans, called EXCESP. The database contains both experimentally determined and computationally predicted interactions among all type-I transmembrane proteins in humans. All structural models for these interactions and their binding affinities were further computationally modeled. Moreover, information such as expression levels of each protein in different cell types and its relation to various signaling pathways from other online resources has also been integrated into the database. In summary, the database serves as a valuable addition to the existing online resources for the study of cell surface proteins. It can contribute to the understanding of the functions of cell surface proteins in the era of systems biology.

Keywords: cell surface proteins; computational modeling; extracellular interactome; online database; systems biology.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Computational Biology / methods
  • Humans
  • Membrane Proteins* / genetics
  • Protein Interaction Mapping / methods
  • Signal Transduction
  • Systems Biology*

Substances

  • Membrane Proteins