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Mutations at protein-protein interfaces: Small changes over big surfaces have large impacts on human health.


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Publication Date: 2017-09

Journal Title: Progress in biophysics and molecular biology

ISSN: 0079-6107

Publisher: Elsevier

Volume: 128

Pages: 3-13

Language: English

Type: Article

This Version: VoR

Physical Medium: Print-Electronic

Metadata: Show full item record

Citation: Jubb, H., Pandurangan, A. P., Turner, M. A., Ochoa-Montaño, B., Blundell, T. L., & Ascher, D. B. (2017). Mutations at protein-protein interfaces: Small changes over big surfaces have large impacts on human health

Progress in biophysics and molecular biology, 128 3-13. https://doi.org/10.1016/j.pbiomolbio.2016.10.002

Abstract: Many essential biological processes including cell regulation and signalling are mediated through the assembly of protein complexes. Changes to protein-protein interaction (PPI) interfaces can affect the formation of multiprotein complexes, and consequently lead to disruptions in interconnected networks of PPIs within and between cells, further leading to phenotypic changes as functional interactions are created or disrupted. Mutations altering PPIs have been linked to the development of genetic diseases including cancer and rare Mendelian diseases, and to the development of drug resistance. The importance of these protein mutations has led to the development of many resources for understanding and predicting their effects. We propose that a better understanding of how these mutations affect the structure, function, and formation of multiprotein complexes provides novel opportunities for tackling them, including the development of small-molecule drugs targeted specifically to mutated PPIs.

Sponsorship: H.J. is currently funded by an Astex Pharmaceuticals Sustaining Innovation Postdoctoral Fellowship hosted at the Wellcome Trust Sanger Institute. M.A.T was supported by scholarships from Promega Corporation, as well as the College of Agricultural and Life Sciences and the Department of Biochemistry at the University of Wisconsin-Madison, USA. B.O.M was supported by the Bill and Melinda Gates Foundation. D.B.A is the recipient of a C. J. Martin Research Fellowship from the National Health and Medical Research Council of Australia (APP1072476) and is funded by the Wellcome Trust and Jack Brockhoff Foundation (JBF 4186, 2016). T.L.B. receives funding from the University of Cambridge and The Wellcome Trust for facilities and support.

Embargo Lift Date: 2100-01-01

Identifiers:

External DOI: https://doi.org/10.1016/j.pbiomolbio.2016.10.002

This record's URL: https://www.repository.cam.ac.uk/handle/1810/261808



Rights:

Licence:

http://creativecommons.org/licenses/by/4.0/





Autor: Jubb, HarryPandurangan, Arun PrasadTurner, Meghan AOchoa-Montaño, Bernardo Blundell, Tom Leon Ascher, David Benjamin

Fuente: https://www.repository.cam.ac.uk/handle/1810/261808



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