More Diversity Yields a Clearer Picture into the Architecture of the Protein Kinase Domain

Markus A. Seeliger

doi:10.1016/j.cels.2018.10.002

More Diversity Yields a Clearer Picture into the Architecture of the Protein Kinase Domain

Markus A. Seeliger

Pharmacological Sciences

Research output: Contribution to journal › Short survey › peer-review

1 Scopus citations

Abstract

Co-evolution analysis reveals which amino acids within the protein kinase domain are working together to mediate catalysis, regulation, and substrate binding. Co-evolution analysis reveals which amino acids within the protein kinase domain are working together to mediate catalysis, regulation, and substrate binding.

Original language	English
Pages (from-to)	356-357
Number of pages	2
Journal	Cell Systems
Volume	7
Issue number	4
DOIs	https://doi.org/10.1016/j.cels.2018.10.002
State	Published - Oct 24 2018

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10.1016/j.cels.2018.10.002

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abstract = "Co-evolution analysis reveals which amino acids within the protein kinase domain are working together to mediate catalysis, regulation, and substrate binding. Co-evolution analysis reveals which amino acids within the protein kinase domain are working together to mediate catalysis, regulation, and substrate binding.",

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M3 - Short survey

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More Diversity Yields a Clearer Picture into the Architecture of the Protein Kinase Domain

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