2KOX
NMR residual dipolar couplings identify long range correlated motions in the backbone of the protein ubiquitin
Summary for 2KOX
| Entry DOI | 10.2210/pdb2kox/pdb |
| Related | 1d3z 1ubq 2k39 2nr2 |
| Descriptor | Ubiquitin (1 entity in total) |
| Functional Keywords | ubiquitin, residual dipolar coupling, simulated annealing, isopeptide bond, nucleus, phosphoprotein, signaling protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 8576.83 |
| Authors | Fenwick, R.B.,Richter, B.,Lee, D.,Walter, K.F.A.,Milovanovic, D.,Becker, S.,Lakomek, N.A.,Griesinger, C.,Salvatella, X. (deposition date: 2009-10-02, release date: 2011-06-08, Last modification date: 2024-05-01) |
| Primary citation | Fenwick, R.B.,Esteban-Martin, S.,Richter, B.,Lee, D.,Walter, K.F.A.,Milovanovic, D.,Becker, S.,Lakomek, N.A.,Griesinger, C.,Salvatella, X. Weak Long-Range Correlated Motions in a Surface Patch of Ubiquitin Involved in Molecular Recognition J.Am.Chem.Soc., 2011 Cited by PubMed Abstract: Long-range correlated motions in proteins are candidate mechanisms for processes that require information transfer across protein structures, such as allostery and signal transduction. However, the observation of backbone correlations between distant residues has remained elusive, and only local correlations have been revealed using residual dipolar couplings measured by NMR spectroscopy. In this work, we experimentally identified and characterized collective motions spanning four β-strands separated by up to 15 Å in ubiquitin. The observed correlations link molecular recognition sites and result from concerted conformational changes that are in part mediated by the hydrogen-bonding network. PubMed: 21634390DOI: 10.1021/ja200461n PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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