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Open Access Research article

The Sam domain of the lipid phosphatase Ship2 adopts a common model to interact with Arap3-Sam and EphA2-Sam

Marilisa Leone, Jason Cellitti and Maurizio Pellecchia*

Author Affiliations

Burnham Institute for Medical Research, La Jolla, California, USA

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BMC Structural Biology 2009, 9:59  doi:10.1186/1472-6807-9-59

Published: 18 September 2009

Additional files

Additional file 1:

ITC control experiment. Calorimetric curve showing the titration of the Shiptide versus buffer.

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Additional file 2:

Chemical shift perturbation studies with the Arap3-Sam mutant. The comparison of 2D [1H, 15N]-HSQC spectra of 15N labeled Arap3-Sam mutant in absence and presence of unlabeled Ship2-Sam and the overlay of 2D [1H, 15N]-HSQC spectra of 15N labeled Ship2-Sam in absence and presence of unlabeled Arap3-Sam mutant, are reported.

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Additional file 3:

Displacement experiment. The 2D [1H, 15N]-HSQC spectra of 15N labeled EphA2-Sam in its apo form, bound to Ship2-Sam and in presence of both Ship2-Sam and Arap3-Sam, are shown.

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Additional file 4:

Protein sequences. The amino acid sequence of the wild-type and mutant proteins, we used in this study, are here listed.

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