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Structure paper

TitleStructural basis for conformational plasticity in the GTPase domain of the Parkinson's disease-associated protein LRRK2
Journal, issue, pagesTo Be Published
Publish dateApr 11, 2019 (structure data deposition date)
AuthorsWu, C.X. / Liao, J. / Park, Y. / Hoang, N.C. / Engel, V.A. / Sanishvili, R. / Takagi, Y. / Johnson, S.M. / Wang, M. / Federici, M. ...Wu, C.X. / Liao, J. / Park, Y. / Hoang, N.C. / Engel, V.A. / Sanishvili, R. / Takagi, Y. / Johnson, S.M. / Wang, M. / Federici, M. / Nichols, R.J. / Cookson, M.R. / Hoang, Q.Q.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.6 - 1.968 Å
Structure data

PDB-6oje:
Dimeric structure of LRRK2 GTPase domain
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-6ojf:
Dimeric structure of LRRK2 GTPase domain
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-6xaf:
1.9A crystal structure of the GTPase domain of Parkinson's disease-associated protein LRRK2 carrying R1398H
Method: X-RAY DIFFRACTION / Resolution: 1.968 Å

Chemicals

ChemComp-MG:
Unknown entry

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

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / Parkinson's disease / LRRK2 / GTPase / Dimer / InterSwitch / complex

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