Evaluating the therapeutic viability of bacterially expressed human TLK1B-kinase domain for cancer drug design

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dc.contributor.author Johnson, Delna
dc.contributor.author Hussain, Javeena
dc.contributor.author Bhoir, Siddhant
dc.contributor.author Sahsrawat, Parul
dc.contributor.author Hans, Tanya
dc.contributor.author Vaishali, C.
dc.contributor.author Thiruvenkatam, Vijay
dc.contributor.author Kirubakaran, Sivapriya
dc.date.accessioned 2022-03-10T14:08:59Z
dc.date.available 2022-03-10T14:08:59Z
dc.date.issued 2022-02
dc.identifier.citation Johnson, Delna; Hussain, Javeena; Bhoir, Siddhant; Sahsrawat, Parul; Hans, Tanya; Vaishali, C.; Thiruvenkatam, Vijay and Kirubakaran,Sivapriya, "Evaluating the therapeutic viability of bacterially expressed human TLK1B-kinase domain for cancer drug design", Research Square, Research Square Company, DOI: 10.21203/rs.3.rs-1314176/v1, Feb. 2022. en_US
dc.identifier.issn
dc.identifier.uri https://doi.org/10.21203/rs.3.rs-1314176/v1
dc.identifier.uri https://repository.iitgn.ac.in/handle/123456789/7560
dc.description.abstract The role of protein kinases is vital in diverse cellular functions. The alterations in the expression patterns of protein kinases often implicate human cancer initiation and progression. Human Tousled-like kinases (TLKs) are evolutionary kinases found in the cell signalling pathway and are involved in DNA repair, replication and chromosomal integrity. The direct association of TLKs to cancer; amplification of both TLK1/1B and TLK2 has made them viable molecular targets for anticancer therapy. Several reports demonstrate numerous functions of TLKs in development of disease via different interacting partners. However, a detailed understanding of its substrates and regulation has yet remained elusive. In this report, through preliminary biophysical and biochemical characterization, we investigate and determine the usability of the recombinant Human Tousled-like Kinase 1B-Kinase Domain (hTLK1B-KD) purified from Escherichia coli for structural and functional studies. By illustrating hTLK1B-KD as an example, our attempts to generate a stable, homogenously dephosphorylated, and catalytically active hTLK1B-KD in high yields is utilizing a bacteriophage ? protein phosphatase (LPP) coexpression system represents a fundamental step towards the structure-based design of TLK-specific inhibitors.
dc.description.statementofresponsibility by Delna Johnson, Javeena Hussain, Siddhant Bhoir, Parul Sahsrawat, Tanya Hans, C. Vaishali, Vijay Thiruvenkatam and Sivapriya Kirubakaran
dc.format.extent
dc.language.iso en_US en_US
dc.publisher Research Square Company en_US
dc.subject Protein kinases en_US
dc.subject Tousled-like kinases en_US
dc.subject Anticancer therapy en_US
dc.subject Escherichia coli en_US
dc.subject LPP en_US
dc.title Evaluating the therapeutic viability of bacterially expressed human TLK1B-kinase domain for cancer drug design en_US
dc.type Pre-Print en_US
dc.relation.journal Research Square


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