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Structure paper

TitleBtk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms.
Journal, issue, pagesNat Commun, Vol. 11, Page 2319-2319, Year 2020
Publish dateOct 4, 2018 (structure data deposition date)
AuthorsDuarte, D.P. / Lamontanara, A.J. / La Sala, G. / Jeong, S. / Sohn, Y.K. / Panjkovich, A. / Georgeon, S. / Kukenshoner, T. / Marcaida, M.J. / Pojer, F. ...Duarte, D.P. / Lamontanara, A.J. / La Sala, G. / Jeong, S. / Sohn, Y.K. / Panjkovich, A. / Georgeon, S. / Kukenshoner, T. / Marcaida, M.J. / Pojer, F. / De Vivo, M. / Svergun, D. / Kim, H.S. / Dal Peraro, M. / Hantschel, O.
External linksNat Commun / PubMed:32385234
MethodsX-ray diffraction
Resolution2.102 Å
Structure data

PDB-6htf:
Crystal structure of human Btk SH2 domain bound to rF10 repebody
Method: X-RAY DIFFRACTION / Resolution: 2.102 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsSIGNALING PROTEIN / Repebody / SH2 domain / Btk

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