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Structure paper

TitleGTP hydrolysis is modulated by Arg34 in the RASopathy-associated KRASP34R.
Journal, issue, pagesBirth Defects Res, Vol. 112, Page 708-717, Year 2020
Publish dateOct 16, 2018 (structure data deposition date)
AuthorsBera, A.K. / Lu, J. / Lu, C. / Li, L. / Gondi, S. / Yan, W. / Nelson, A. / Zhang, G. / Westover, K.D.
External linksBirth Defects Res / PubMed:32187889
MethodsX-ray diffraction
Resolution1.49 - 2.15 Å
Structure data

PDB-6ms9:
GDP-bound KRAS P34R mutant
Method: X-RAY DIFFRACTION / Resolution: 1.49 Å

PDB-6mta:
KRAS P34R mutant structure in complex with GTP analogue
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

PDB-6o36:
Crystal structure of human KRAS P34R mutant in complex with GNP
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-6o46:
Crystal structure of human KRAS P34R mutant in complex with GNP and Phosphate
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-GNP:
PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / GppNHp, GMPPNP, energy-carrying molecule analogue*YM

ChemComp-PO4:
PHOSPHATE ION

Source
  • homo sapiens (human)
KeywordsHYDROLASE / GTPASE KRAS HYDROLYSIS / small GTPase / signal transduction / GNP binding

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