1U42
Crystal structure of MLAM mutant of dimerisation domain of NF-kB p50 transcription factor
Summary for 1U42
| Entry DOI | 10.2210/pdb1u42/pdb |
| Related | 1U36 1U3J 1U3Y 1U3Z 1U41 |
| Descriptor | Nuclear factor NF-kappa-B p105 subunit (2 entities in total) |
| Functional Keywords | transcription factor; nf-kb; dimerization domain; intertwined folding, transcription |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Nucleus. Isoform 5: Cytoplasm. Isoform 6: Nucleus. Isoform 7: Nucleus: P25799 |
| Total number of polymer chains | 1 |
| Total formula weight | 12256.92 |
| Authors | Chirgadze, D.Y.,Demydchuk, M.,Becker, M.,Moran, S.,Paoli, M. (deposition date: 2004-07-23, release date: 2004-08-17, Last modification date: 2023-08-23) |
| Primary citation | Chirgadze, D.Y.,Demydchuk, M.,Becker, M.,Moran, S.,Paoli, M. Snapshot of Protein Structure Evolution Reveals Conservation of Functional Dimerization through Intertwined Folding Structure, 12:1489-1494, 2004 Cited by PubMed Abstract: Protein-protein interactions govern a wide range of cellular processes. Molecular recognition responsible for homodimerization and heterodimerization in the rel/NF-kappaB family of eukaryotic transcription factors relies on a small cluster of hydrophobic residues. We have carried out a structural analysis of six NF-kappaB p50 dimer interface mutants; one of them revealed a remarkable alteration. One or possibly both its mutations cause a switch into an intertwined dimer, in which the molecular partners exchange nearly half of their fold. In spite of the extensive swapping of secondary structure elements, the topology within each counterpart is preserved, with a very similar overall structure and minimal changes at the interface. Thus intertwining rescues structure and function from a destabilizing mutation. Since the mutants originate from a directed evolution experiment and are functional, the data provide an evolutionary snapshot of how a protein structure can respond to mutations while maintaining a functional molecular architecture. PubMed: 15296742DOI: 10.1016/j.str.2004.06.011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.699 Å) |
Structure validation
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