4HP4
Crystal structure of PAS domain from the fruit-fly ELK potassium channel
Summary for 4HP4
| Entry DOI | 10.2210/pdb4hp4/pdb |
| Related | 1BYW 4HOI 4HP9 4HQA |
| Descriptor | Eag-like K[+] channel, SULFATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | potassium channel domain, pas domain, transport protein |
| Biological source | Drosophila melanogaster (Fruit fly) |
| Total number of polymer chains | 2 |
| Total formula weight | 30523.03 |
| Authors | Adaixo, R.,Morais-Cabral, J.H. (deposition date: 2012-10-23, release date: 2013-03-27, Last modification date: 2023-11-08) |
| Primary citation | Adaixo, R.,Harley, C.A.,Castro-Rodrigues, A.F.,Morais-Cabral, J.H. Structural properties of PAS domains from the KCNH potassium channels Plos One, 8:e59265-e59265, 2013 Cited by PubMed Abstract: KCNH channels form an important family of voltage gated potassium channels. These channels include a N-terminal Per-Arnt-Sim (PAS) domain with unknown function. In other proteins PAS domains are implicated in cellular responses to environmental queues through small molecule binding or involvement in signaling cascades. To better understand their role we characterized the structural properties of several channel PAS domains. We determined high resolution structures of PAS domains from the mouse EAG (mEAG), drosophila ELK (dELK) and human ERG (hERG) channels and also of the hERG domain without the first nine amino acids. We analyzed these structures for features connected to ligand binding and signaling in other PAS domains. In particular, we have found cavities in the hERG and mEAG structures that share similarities with the ligand binding sites from other PAS domains. These cavities are lined by polar and apolar chemical groups and display potential flexibility in their volume. We have also found that the hydrophobic patch on the domain β-sheet is a conserved feature and appears to drive the formation of protein-protein contacts. In addition, the structures of the dELK domain and of the truncated hERG domain revealed the presence of N-terminal helices. These helices are equivalent to the helix described in the hERG NMR structures and are known to be important for channel function. Overall, these channel domains retain many of the PAS domain characteristics known to be important for cell signaling. PubMed: 23555008DOI: 10.1371/journal.pone.0059265 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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