2RPQ
Solution Structure of a SUMO-interacting motif of MBD1-containing chromatin-associated factor 1 bound to SUMO-3
Summary for 2RPQ
| Entry DOI | 10.2210/pdb2rpq/pdb |
| Descriptor | Small ubiquitin-related modifier 2, Activating transcription factor 7-interacting protein 1 (2 entities in total) |
| Functional Keywords | sumo, sim, nucleus, ubl conjugation pathway, activator, host-virus interaction, phosphoprotein, repressor, transcription, transcription regulation |
| Biological source | Homo sapiens (Human) More |
| Cellular location | Nucleus: P61956 Q6VMQ6 |
| Total number of polymer chains | 2 |
| Total formula weight | 15540.06 |
| Authors | Sekiyama, N.,Ikegami, T.,Yamane, T.,Ikeguchi, M.,Uchimura, Y.,Baba, D.,Ariyoshi, M.,Tochio, H.,Saitoh, H.,Shirakawa, M. (deposition date: 2008-07-07, release date: 2008-10-07, Last modification date: 2024-05-01) |
| Primary citation | Sekiyama, N.,Ikegami, T.,Yamane, T.,Ikeguchi, M.,Uchimura, Y.,Baba, D.,Ariyoshi, M.,Tochio, H.,Saitoh, H.,Shirakawa, M. Structure of the small ubiquitin-like modifier (SUMO)-interacting motif of MBD1-containing chromatin-associated factor 1 bound to SUMO-3 J.Biol.Chem., 283:35966-35975, 2008 Cited by PubMed Abstract: Post-translational modification by small ubiquitin-like modifier (SUMO) proteins has been implicated in the regulation of a variety of cellular events. The functions of sumoylation are often mediated by downstream effector proteins harboring SUMO-interacting motifs (SIMs) that are composed of a hydrophobic core and a stretch of acidic residues. MBD1-containing chromatin-associated factor 1 (MCAF1), a transcription repressor, interacts with SUMO-2/3 and SUMO-1, with a preference for SUMO-2/3. We used NMR spectroscopy to solve the solution structure of the SIM of MCAF1 bound to SUMO-3. The hydrophobic core of the SIM forms a parallel beta-sheet pairing with strand beta2 of SUMO-3, whereas its C-terminal acidic stretch seems to mediate electrostatic interactions with a surface area formed by basic residues of SUMO-3. The significance of these electrostatic interactions was shown by mutations of both SUMO-3 and MCAF1. The present structural and biochemical data suggest that the acidic stretch of the SIM of MCAF1 plays an important role in the binding to SUMO-3. PubMed: 18842587DOI: 10.1074/jbc.M802528200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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