2LAS
Molecular Determinants of Paralogue-Specific SUMO-SIM Recognition
Summary for 2LAS
| Entry DOI | 10.2210/pdb2las/pdb |
| Related | 2ASQ |
| NMR Information | BMRB: 17536 |
| Descriptor | Small ubiquitin-related modifier 1, M-IR2_peptide (2 entities in total) |
| Functional Keywords | ranbp2, post-translational modification, transcription |
| Biological source | Homo sapiens (human) More |
| Cellular location | Nucleus membrane: P63165 |
| Total number of polymer chains | 2 |
| Total formula weight | 13191.86 |
| Authors | Namanja, A.,Li, Y.,Su, Y.,Wong, S.,Lu, J.,Colson, L.,Wu, C.,Li, S.,Chen, Y. (deposition date: 2011-03-20, release date: 2011-12-14, Last modification date: 2024-05-15) |
| Primary citation | Namanja, A.T.,Li, Y.J.,Su, Y.,Wong, S.,Lu, J.,Colson, L.T.,Wu, C.,Li, S.S.,Chen, Y. Insights into High Affinity Small Ubiquitin-like Modifier (SUMO) Recognition by SUMO-interacting Motifs (SIMs) Revealed by a Combination of NMR and Peptide Array Analysis. J.Biol.Chem., 287:3231-3240, 2012 Cited by PubMed Abstract: The small ubiquitin-like modifiers (SUMOs) regulate many essential cellular functions. Only one type of SUMO-interacting motif (SIM) has been identified that can extend the β-sheet of SUMO as either a parallel or an antiparallel strand. The molecular determinants of the bound orientation and paralogue specificity of a SIM are unclear. To address this question, we have conducted structural studies of SUMO1 in complex with a SUMO1-specific SIM that binds to SUMO1 with high affinity without post-translational modifications using nuclear magnetic resonance methods. In addition, the SIM sequence requirements have been investigated by peptide arrays in comparison with another high affinity SIM that binds in the opposing orientation. We found that antiparallel binding SIMs tolerate more diverse sequences, whereas the parallel binding SIMs prefer the more strict sequences consisting of (I/V)DLT that have a preference in high affinity SUMO2 and -3 binding. Comparison of two high affinity SUMO1-binding SIMs that bind in opposing orientations has revealed common SUMO1-specific interactions needed for high affinity binding. This study has significantly advanced our understanding of the molecular determinants underlining SUMO-SIM recognition. PubMed: 22147707DOI: 10.1074/jbc.M111.293118 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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