Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms
Constitutive Btk signaling drives several B-cell cancers. Here the authors demonstrate key allosteric intramolecular interactions between the SH2 domain and the kinase domain of Btk, and propose an alternative approach for inhibition of both wild-type and tyrosine kinase inhibitor-resistant Btk.
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Nature Portfolio
2020
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oai:doaj.org-article:35d89457e02f4b24aac8c29d226477992021-12-02T16:49:44ZBtk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms10.1038/s41467-020-16128-52041-1723https://doaj.org/article/35d89457e02f4b24aac8c29d226477992020-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-16128-5https://doaj.org/toc/2041-1723Constitutive Btk signaling drives several B-cell cancers. Here the authors demonstrate key allosteric intramolecular interactions between the SH2 domain and the kinase domain of Btk, and propose an alternative approach for inhibition of both wild-type and tyrosine kinase inhibitor-resistant Btk.Daniel P. DuarteAllan J. LamontanaraGiuseppina La SalaSukyo JeongYoo-Kyoung SohnAlejandro PanjkovichSandrine GeorgeonTim KükenshönerMaria J. MarcaidaFlorence PojerMarco De VivoDmitri SvergunHak-Sung KimMatteo Dal PeraroOliver HantschelNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-15 (2020) |
| institution |
DOAJ |
| collection |
DOAJ |
| language |
EN |
| topic |
Science Q |
| spellingShingle |
Science Q Daniel P. Duarte Allan J. Lamontanara Giuseppina La Sala Sukyo Jeong Yoo-Kyoung Sohn Alejandro Panjkovich Sandrine Georgeon Tim Kükenshöner Maria J. Marcaida Florence Pojer Marco De Vivo Dmitri Svergun Hak-Sung Kim Matteo Dal Peraro Oliver Hantschel Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms |
| description |
Constitutive Btk signaling drives several B-cell cancers. Here the authors demonstrate key allosteric intramolecular interactions between the SH2 domain and the kinase domain of Btk, and propose an alternative approach for inhibition of both wild-type and tyrosine kinase inhibitor-resistant Btk. |
| format |
article |
| author |
Daniel P. Duarte Allan J. Lamontanara Giuseppina La Sala Sukyo Jeong Yoo-Kyoung Sohn Alejandro Panjkovich Sandrine Georgeon Tim Kükenshöner Maria J. Marcaida Florence Pojer Marco De Vivo Dmitri Svergun Hak-Sung Kim Matteo Dal Peraro Oliver Hantschel |
| author_facet |
Daniel P. Duarte Allan J. Lamontanara Giuseppina La Sala Sukyo Jeong Yoo-Kyoung Sohn Alejandro Panjkovich Sandrine Georgeon Tim Kükenshöner Maria J. Marcaida Florence Pojer Marco De Vivo Dmitri Svergun Hak-Sung Kim Matteo Dal Peraro Oliver Hantschel |
| author_sort |
Daniel P. Duarte |
| title |
Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms |
| title_short |
Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms |
| title_full |
Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms |
| title_fullStr |
Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms |
| title_full_unstemmed |
Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms |
| title_sort |
btk sh2-kinase interface is critical for allosteric kinase activation and its targeting inhibits b-cell neoplasms |
| publisher |
Nature Portfolio |
| publishDate |
2020 |
| url |
https://doaj.org/article/35d89457e02f4b24aac8c29d22647799 |
| work_keys_str_mv |
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| _version_ |
1718383208076148736 |