5Z1W
Cryo-EM structure of polycystic kidney disease-like channel PKD2L1
Summary for 5Z1W
| Entry DOI | 10.2210/pdb5z1w/pdb |
| EMDB information | 6877 |
| Descriptor | Polycystic kidney disease 2-like 1 protein, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total) |
| Functional Keywords | channel, cryo-em, membrane protein |
| Biological source | Mus musculus (Mouse) |
| Total number of polymer chains | 4 |
| Total formula weight | 265058.03 |
| Authors | Zhang, Y.Q. (deposition date: 2017-12-28, release date: 2018-03-28, Last modification date: 2025-07-02) |
| Primary citation | Su, Q.,Hu, F.,Liu, Y.,Ge, X.,Mei, C.,Yu, S.,Shen, A.,Zhou, Q.,Yan, C.,Lei, J.,Zhang, Y.,Liu, X.,Wang, T. Cryo-EM structure of the polycystic kidney disease-like channel PKD2L1. Nat Commun, 9:1192-1192, 2018 Cited by PubMed Abstract: PKD2L1, also termed TRPP3 from the TRPP subfamily (polycystic TRP channels), is involved in the sour sensation and other pH-dependent processes. PKD2L1 is believed to be a nonselective cation channel that can be regulated by voltage, protons, and calcium. Despite its considerable importance, the molecular mechanisms underlying PKD2L1 regulations are largely unknown. Here, we determine the PKD2L1 atomic structure at 3.38 Å resolution by cryo-electron microscopy, whereby side chains of nearly all residues are assigned. Unlike its ortholog PKD2, the pore helix (PH) and transmembrane segment 6 (S6) of PKD2L1, which are involved in upper and lower-gate opening, adopt an open conformation. Structural comparisons of PKD2L1 with a PKD2-based homologous model indicate that the pore domain dilation is coupled to conformational changes of voltage-sensing domains (VSDs) via a series of π-π interactions, suggesting a potential PKD2L1 gating mechanism. PubMed: 29567962DOI: 10.1038/s41467-018-03606-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.38 Å) |
Structure validation
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