7Q71
The crystallographic structure of the Ligand Binding domain of the NR7 nuclear receptor from the amphioxus Branchiostoma lanceolatum
Summary for 7Q71
| Entry DOI | 10.2210/pdb7q71/pdb |
| Descriptor | Nuclear hormone receptor 7, CHLORIDE ION, PHOSPHATE ION, ... (4 entities in total) |
| Functional Keywords | nuclear receptor, ligand binding domain, amphioxus, heterodimerization, transcription |
| Biological source | Branchiostoma lanceolatum (Common lancelet, Amphioxus lanceolatum) |
| Total number of polymer chains | 1 |
| Total formula weight | 26834.82 |
| Authors | Billas, I.M.L.,McEwen, A.G.,Hazemann, I.,Moras, D.,Laudet, V. (deposition date: 2021-11-09, release date: 2022-09-14, Last modification date: 2024-01-31) |
| Primary citation | Beinsteiner, B.,Markov, G.V.,Bourguet, M.,McEwen, A.G.,Erb, S.,Patel, A.K.M.,El Khaloufi El Khaddar, F.Z.,Lecroisey, C.,Holzer, G.,Essabri, K.,Hazemann, I.,Hamiche, A.,Cianferani, S.,Moras, D.,Laudet, V.,Billas, I.M.L. A novel nuclear receptor subfamily enlightens the origin of heterodimerization. Bmc Biol., 20:217-217, 2022 Cited by PubMed Abstract: Nuclear receptors are transcription factors of central importance in human biology and associated diseases. Much of the knowledge related to their major functions, such as ligand and DNA binding or dimerization, derives from functional studies undertaken in classical model animals. It has become evident, however, that a deeper understanding of these molecular functions requires uncovering how these characteristics originated and diversified during evolution, by looking at more species. In particular, the comprehension of how dimerization evolved from ancestral homodimers to a more sophisticated state of heterodimers has been missing, due to a too narrow phylogenetic sampling. Here, we experimentally and phylogenetically define the evolutionary trajectory of nuclear receptor dimerization by analyzing a novel NR7 subgroup, present in various metazoan groups, including cnidarians, annelids, mollusks, sea urchins, and amphioxus, but lost in vertebrates, arthropods, and nematodes. PubMed: 36199108DOI: 10.1186/s12915-022-01413-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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