Site-directed mutagenesis in the P-domain of calreticulin transacylase identifies Lys-207 as the active site residue

In silico-docking studies from previous work have suggested that Lys-206 and lys-207 of calreticulin (CR) play a pivotal key role in its well-established transacetylation activity. To experimentally validate this prediction, we introduced three mutations at lysine residues of P-domain of CR: K → A,...

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Detalhes bibliográficos
Publicado no:3 Biotech
Main Authors: Joshi, Rini, Singh, Prabhjot, Sharma, Naresh K., Ponnan, Prija, Saluja, Daman, Gambhir, Jasvinder K., Rawat, Diwan S., Parmar, Virinder S., Dwarakanath, Bilkere S., Prasad, Ashok K., Raj, Hanumantharao G.
Formato: Artigo
Idioma:Inglês
Publicado em: Springer International Publishing 2021
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Original Article
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC7859019/
https://ncbi.nlm.nih.gov/pubmed/33585151
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1007/s13205-021-02659-1
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