Dynamic control of selectivity in the ubiquitination pathway revealed by an ASP to GLU substitution in an intra-molecular salt-bridge network

Ubiquitination relies on a subtle balance between selectivity and promiscuity achieved through specific interactions between ubiquitin-conjugating enzymes (E2s) and ubiquitin ligases (E3s). Here, we report how a single aspartic to glutamic acid substitution acts as a dynamic switch to tip the select...

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Veröffentlicht in:	PLoS computational biology 2012-11, Vol.8 (11), p.e1002754
Hauptverfasser:	van Wijk, Sjoerd J L, Melquiond, Adrien S J, de Vries, Sjoerd J, Timmers, H Th Marc, Bonvin, Alexandre M J J
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino Acid Substitution Aspartic Acid - chemistry Aspartic Acid - genetics Aspartic Acid - metabolism Bioinformatics Biology Chemistry Computational Biology Computer Science Glutamate Glutamic Acid - chemistry Glutamic Acid - genetics Glutamic Acid - metabolism Health aspects Humans Hydrogen Bonding Models, Molecular Molecular dynamics Molecular Sequence Data Mutagenesis Physiological aspects Promiscuity Protein Binding Protein Conformation Protein Structure, Tertiary Proteins Reproducibility of Results Sequence Alignment Static Electricity Two-Hybrid System Techniques Ubiquitin-Conjugating Enzymes - chemistry Ubiquitin-Conjugating Enzymes - genetics Ubiquitin-Conjugating Enzymes - metabolism Ubiquitin-proteasome system Ubiquitin-Protein Ligases - chemistry Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - metabolism Ubiquitination - genetics Ubiquitination - physiology
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