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Structure paper

TitleMapping the structure and conformational movements of proteins with transition metal ion FRET.
Journal, issue, pagesNat. Methods, Vol. 6, Page 532-537, Year 2009
Publish dateOct 8, 2008 (structure data deposition date)
AuthorsTaraska, J.W. / Puljung, M.C. / Olivier, N.B. / Flynn, G.E. / Zagotta, W.N.
External linksNat. Methods / PubMed:19525958
MethodsX-ray diffraction
Resolution1.9 - 2.4 Å
Structure data

PDB-3etq:
X-ray structure of cysteine-free fragment of mHCN2 C-terminal region from amino acids 443-630 including C508N, C584S, and C601S mutations
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-3ffq:
HCN2I 443-640 apo-state
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

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

ChemComp-HOH:
WATER

ChemComp-BR:
BROMIDE ION

Source
  • mus musculus (house mouse)
KeywordsTRANSPORT PROTEIN / HCN / ion channel / cAMP / Cyclic nucleotide binding domain / beta roll / C-linker / cAMP-binding / Glycoprotein / Ion transport / Ionic channel / Membrane / Nucleotide-binding / Phosphoprotein / Potassium / Potassium channel / Potassium transport / Sodium / Sodium channel / Sodium transport / Transmembrane / Transport / Voltage-gated channel / METAL TRANSPORT

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