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TitleStructure and regulation of full-length human leucine-rich repeat kinase 1.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 4797, Year 2023
Publish dateAug 9, 2023
AuthorsRiley D Metcalfe / Juliana A Martinez Fiesco / Luis Bonet-Ponce / Jillian H Kluss / Mark R Cookson / Ping Zhang /
PubMed AbstractThe human leucine-rich repeat kinases (LRRKs), LRRK1 and LRRK2 are large and unusually complex multi-domain kinases, which regulate fundamental cellular processes and have been implicated in human ...The human leucine-rich repeat kinases (LRRKs), LRRK1 and LRRK2 are large and unusually complex multi-domain kinases, which regulate fundamental cellular processes and have been implicated in human disease. Structures of LRRK2 have recently been determined, but the structure and molecular mechanisms regulating the activity of the LRRK1 as well as differences in the regulation of LRRK1 and LRRK2 remain unclear. Here, we report a cryo-EM structure of the LRRK1 monomer and a lower-resolution cryo-EM map of the LRRK1 dimer. The monomer structure, in which the kinase is in an inactive conformation, reveals key interdomain interfaces that control kinase activity as we validate experimentally. Both the LRRK1 monomer and dimer are structurally distinct compared to LRRK2. Overall, our results provide structural insights into the activation of the human LRRKs, which advance our understanding of their physiological and pathological roles.
External linksNat Commun / PubMed:37558661 / PubMed Central
MethodsEM (single particle)
Resolution3.78 - 6.38 Å
Structure data

EMDB-28949: Leucine-rich repeat kinase 1 monomer, global refinement
Method: EM (single particle) / Resolution: 3.92 Å

28950

8fac

EMDB-28950, PDB-8fac:
Structure of the leucine-rich repeat kinase 1 monomer
Method: EM (single particle) / Resolution: 3.92 Å

EMDB-28951: Leucine-rich repeat kinase 1 monomer, focused refinement on C-terminal region
Method: EM (single particle) / Resolution: 3.78 Å

EMDB-28952: Cryo-EM map of the LRRK1 dimer
Method: EM (single particle) / Resolution: 6.38 Å

Chemicals

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

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / kinase / LRRK / multi-domain protein / GTPase

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