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TitleStructural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase.
Journal, issue, pagesNat Commun, Vol. 8, Issue 1, Page 2101, Year 2017
Publish dateDec 13, 2017
AuthorsSina Reckel / Charlotte Gehin / Delphine Tardivon / Sandrine Georgeon / Tim Kükenshöner / Frank Löhr / Akiko Koide / Lena Buchner / Alejandro Panjkovich / Aline Reynaud / Sara Pinho / Barbara Gerig / Dmitri Svergun / Florence Pojer / Peter Güntert / Volker Dötsch / Shohei Koide / Anne-Claude Gavin / Oliver Hantschel /
PubMed AbstractThe two isoforms of the Bcr-Abl tyrosine kinase, p210 and p190, are associated with different leukemias and have a dramatically different signaling network, despite similar kinase activity. To ...The two isoforms of the Bcr-Abl tyrosine kinase, p210 and p190, are associated with different leukemias and have a dramatically different signaling network, despite similar kinase activity. To provide a molecular rationale for these observations, we study the Dbl-homology (DH) and Pleckstrin-homology (PH) domains of Bcr-Abl p210, which constitute the only structural differences to p190. Here we report high-resolution structures of the DH and PH domains and characterize conformations of the DH-PH unit in solution. Our structural and functional analyses show no evidence that the DH domain acts as a guanine nucleotide exchange factor, whereas the PH domain binds to various phosphatidylinositol-phosphates. PH-domain mutants alter subcellular localization and result in decreased interactions with p210-selective interaction partners. Hence, the PH domain, but not the DH domain, plays an important role in the formation of the differential p210 and p190 Bcr-Abl signaling networks.
External linksNat Commun / PubMed:29235475 / PubMed Central
MethodsSAS (X-ray synchrotron) / NMR (solution) / X-ray diffraction
Resolution1.647 - 1.652 Å
Structure data

SASDC26:
DH-PH - Dbl-homology domain (DH) and Pleckstrin-homology (PH) of Bcr-Abl tyrosine kinase p210
Method: SAXS/SANS

SASDC36:
DH - Dbl-homology domain of Bcr-Abl tyrosine kinase p210
Method: SAXS/SANS

SASDC46:
PH - Pleckstrin-homology domain of Bcr-Abl tyrosine kinase p210
Method: SAXS/SANS

PDB-5n6r:
Solution structure of the Dbl-homology domain of Bcr-Abl
Method: SOLUTION NMR

PDB-5n7e:
Crystal structure of the Dbl-homology domain of Bcr-Abl in complex with monobody Mb(Bcr-DH_4).
Method: X-RAY DIFFRACTION / Resolution: 1.647 Å

PDB-5oc7:
Crystal structure of the pleckstrin-homology domain of Bcr-Abl in complex with monobody Mb(Bcr-PH_4).
Method: X-RAY DIFFRACTION / Resolution: 1.652 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-IP2:
D-MYO-INOSITOL-4,5-BISPHOSPHATE

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsSIGNALING PROTEIN / Dbl-homology / helical bundle / Bcr-Abl / leukemia / transferase / monobody / pleckstrin-homology / phosphoinositide-binding

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