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TitleDisrupting the Allosteric Interaction between the Plasmodium falciparum cAMP-dependent Kinase and Its Regulatory Subunit.
Journal, issue, pagesJ. Biol. Chem., Vol. 291, Page 25375-25386, Year 2016
Publish dateMay 31, 2016 (structure data deposition date)
AuthorsLittler, D.R. / Bullen, H.E. / Harvey, K.L. / Beddoe, T. / Crabb, B.S. / Rossjohn, J. / Gilson, P.R.
External linksJ. Biol. Chem. / PubMed:27738107
MethodsX-ray diffraction
Resolution1.15 - 2.4 Å
Structure data

PDB-5k8s:
cAMP bound PfPKA-R (297-441)
Method: X-RAY DIFFRACTION / Resolution: 1.15 Å

PDB-5kbf:
cAMP bound PfPKA-R (141-441)
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-5t3n:
Sp-2Cl-cAMPS bound to PKAR CBD2
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

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

ChemComp-HOH:
WATER

ChemComp-IOD:
IODIDE ION

ChemComp-75G:
(2S,4aR,6R,7R,7aS)-6-(6-amino-2-chloro-9H-purin-9-yl)-7-hydroxy-2-sulfanyltetrahydro-2H,4H-2lambda~5~-furo[3,2-d][1,3,2]dioxaphosphinin-2-one

Source
  • plasmodium falciparum (isolate 3d7) (eukaryote)
KeywordsTRANSFERASE / Plasmodium falciparum / PKA / protein kinase A / cAMP / CBD / cyclic nucleotide binding / CNB / regulatory domain / R / PKAR / Plasmodium / cyclic nucleotide / cyclic adenosine monophosphate

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