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Structure paper

TitlePIP2 inhibits pore opening of a CNG channel
Journal, issue, pagesNat Commun, Year 2024
Publish dateJan 26, 2024 (structure data deposition date)
AuthorsThon, O. / Schmidpeter, P.A.M. / Nimigean, C.M.
External linksSearch PubMed
MethodsEM (single particle)
Resolution2.5 - 3 Å
Structure data

PDB-8vt9:
WT SthK in the presence of PIP2 and cAMP
Method: ELECTRON MICROSCOPY / Resolution: 2.9 Å

PDB-8vta:
SthK R120A in the presence of PIP2 and cAMP
Method: ELECTRON MICROSCOPY / Resolution: 3 Å

PDB-8vtb:
SthK R120A R124A in the presence of PIP2 and cAMP
Method: ELECTRON MICROSCOPY / Resolution: 2.5 Å

Chemicals

ChemComp-CMP:
ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE

ChemComp-PT5:
[(2R)-1-octadecanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phospho / phospholipid*YM

ChemComp-PCW:
1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / DOPC, phospholipid*YM

Source
  • spirochaeta thermophila (bacteria)
KeywordsTRANSPORT PROTEIN / cyclic-nucleotide binding / potassium channel / lipid modulation

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