| Literature DB >> 29756279 |
Pallavi M Gosavi1, Megha Jayachandran1, Joel J L Rempillo1, Oleksii Zozulia1, Olga V Makhlynets1, Ivan V Korendovych1.
Abstract
A computationally designed, allosterically regulated catalyst (CaM M144H) produced by substituting a single residue in calmodulin, a non-enzymatic protein, is capable of efficient and site selective post-translational acylation of lysines in peptides with highly diverse sequences. Calmodulin's binding partners are involved in regulating a large number of cellular processes; this new chemical-biology tool will help to identify them and provide structural insight into their interactions with calmodulin.Entities:
Keywords: acyl transfer; allostery; calmodulin; post-translational modifications; protein design
Mesh:
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Year: 2018 PMID: 29756279 PMCID: PMC6394838 DOI: 10.1002/cbic.201800196
Source DB: PubMed Journal: Chembiochem ISSN: 1439-4227 Impact factor: 3.164