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A structure-based model of the c-Myc/Bin1 protein interaction shows alternative splicing of Bin1 and c-Myc phosphorylation are key binding determinants.

Pineda-Lucena A, Ho CS, Mao DY, Sheng Y, Laister RC, Muhandiram R, Lu Y, Seet BT, Katz S, Szyperski T, Penn LZ, Arrowsmith CH,
Journal of Molecular Biology (2005) 351(1):182-94 PublishedPSI:Phase 2  
Northeast Structural Genomics Consortium

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The N terminus of the c-Myc oncoprotein interacts with Bin1, a ubiquitously expressed nucleocytoplasmic protein with features of a tumor suppressor. ...
metabolism chemistry genetics 
Binding Sites Humans Models, Molecular Protein Binding Nuclear Magnetic Resonance, Biomolecular Phosphorylation Carrier Proteins Protein Isoforms Neoplasm Proteins Cell Line Tumor Suppressor Proteins Adaptor Proteins, Signal Transducing Nuclear Proteins Alternative Splicing src Homology Domains Proto-Oncogene Proteins c-myc 
15992821  
10.1016/j.jmb.2005.05.046  
52 (Last update: 11/17/2018 6:15:13pm)  
1MUZ
1MV0
1MV3  
structure  
J Mol Biol. 2005 Aug 5;351(1):182-94.