NMR STRUCTURE OF THE TUMOR SUPPRESSOR BIN1: ALTERNATIVE SPLICING IN MELANOMA AND INTERACTION WITH C-MYC
A structure-based model of the c-Myc/Bin1 protein interaction shows alternative splicing of Bin1 and c-Myc phosphorylation are key binding determinants.
Bridging integrator 1, Amphiphysin-like protein, Amphiphysin II, Box-dependent
GRLDLPPGFMFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKKLEKCRGVFPENFTERV P
NMR STRUCTURE OF THE TUMOR SUPPRESSOR BIN1 (RESIDUES 513-593)
NMR STRUCTURE OF THE TUMOR SUPPRESSOR ISOFORM BIN1 +12A (RESIDUES 301-377, 458-593)
SEQUENCE The protein crystallized by the author contains Lys465 which corresponds to Glu576 in the Swiss-Prot entry O00499. This residue conflict is noted in the database reference.
THIS STRUCTURE WAS DETERMINED USING STANDARD 3D HETERONUCLEAR NMR TECHNIQUES
TUMOR SUPPRESSOR/ONCOPROTEIN, ENDOCYTOSIS/EXOCYTOSIS, TRANSCRIPTION COMPLEX, ENDOCYTOSIS-EXOCYTOSIS
GRLDLPPGFMFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKELEKCRGVFPENFTERV P