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TitleNeutron Diffraction Reveals Hydrogen Bonds Critical for cGMP-Selective Activation: Insights for cGMP-Dependent Protein Kinase Agonist Design.
Journal, issue, pagesBiochemistry, Vol. 53, Page 6725-6727, Year 2014
Publish dateJul 18, 2014 (structure data deposition date)
AuthorsHuang, G.Y. / Gerlits, O.O. / Blakeley, M.P. / Sankaran, B. / Kovalevsky, A.Y. / Kim, C.
External linksBiochemistry / PubMed:25271401
MethodsX-ray diffraction / neutron diffraction
Resolution1.318 - 2.2 Å
Structure data

PDB-4qx5:
Neutron diffraction reveals hydrogen bonds critical for cGMP-selective activation: Insights for PKG agonist design
Method: X-RAY DIFFRACTION / Resolution: 1.318 Å

PDB-4qxk:
Joint X-ray/neutron structure of PKGIbeta in complex with cGMP
Method: X-RAY DIFFRACTION / NEUTRON DIFFRACTION / Resolution: 2.2 Å

Chemicals

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

ChemComp-IOD:
IODIDE ION

ChemComp-HOH:
WATER

ChemComp-PCG:
CYCLIC GUANOSINE MONOPHOSPHATE

ChemComp-NA:
Unknown entry

ChemComp-DOD:
DEUTERATED WATER

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / Phosphate Binding cassette/Cyclic GMP binding domain/PKG / serine/threonine kinase / cyclic GMP / SIGNALING PROTEIN / cyclic GMP (cGMP) / Type I cGMP Dependent Protein Kinase (PKG I) / Cyclic Nucleotide Selectivity / Serine/threonine Protein Kinase / Signal Transduction / Second Messengers / Hydrogen Bonding / Solvent Accessibility

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