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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. ...
chemistry genetics metabolism 
Models, Molecular Nuclear Proteins Cell Line Alternative Splicing Humans Protein Isoforms Adaptor Proteins, Signal Transducing Phosphorylation src Homology Domains Binding Sites Tumor Suppressor Proteins Carrier Proteins Nuclear Magnetic Resonance, Biomolecular Protein Binding Proto-Oncogene Proteins c-myc Neoplasm Proteins 
15992821  
10.1016/j.jmb.2005.05.046  
44 (Last update: 04/01/2017 12:14:05pm)  
1MUZ
1MV0
1MV3  
structure  
J Mol Biol. 2005 Aug 5;351(1):182-94.