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Structure paper

TitleStructural basis of human kinesin-8 function and inhibition.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 114, Issue 45, Page E9539-E9548, Year 2017
Publish dateNov 7, 2017
AuthorsJulia Locke / Agnel Praveen Joseph / Alejandro Peña / Martin M Möckel / Thomas U Mayer / Maya Topf / Carolyn A Moores /
PubMed AbstractKinesin motors play diverse roles in mitosis and are targets for antimitotic drugs. The clinical significance of these motors emphasizes the importance of understanding the molecular basis of their ...Kinesin motors play diverse roles in mitosis and are targets for antimitotic drugs. The clinical significance of these motors emphasizes the importance of understanding the molecular basis of their function. Equally important, investigations into the modes of inhibition of these motors provide crucial information about their molecular mechanisms. Kif18A regulates spindle microtubules through its dual functionality, with microtubule-based stepping and regulation of microtubule dynamics. We investigated the mechanism of Kif18A and its inhibition by the small molecule BTB-1. The Kif18A motor domain drives ATP-dependent plus-end microtubule gliding, and undergoes conformational changes consistent with canonical mechanisms of plus-end-directed motility. The Kif18A motor domain also depolymerizes microtubule plus and minus ends. BTB-1 inhibits both of these microtubule-based Kif18A activities. A reconstruction of BTB-1-bound, microtubule-bound Kif18A, in combination with computational modeling, identified an allosteric BTB-1-binding site near loop5, where it blocks the ATP-dependent conformational changes that we characterized. Strikingly, BTB-1 binding is close to that of well-characterized Kif11 inhibitors that block tight microtubule binding, whereas BTB-1 traps Kif18A on the microtubule. Our work highlights a general mechanism of kinesin inhibition in which small-molecule binding near loop5 prevents a range of conformational changes, blocking motor function.
External linksProc Natl Acad Sci U S A / PubMed:29078367 / PubMed Central
MethodsEM (helical sym.)
Resolution4.8 - 5.5 Å
Structure data

3778

5oam

EMDB-3778, PDB-5oam:
Molecular basis of human kinesin-8 function and inhibition
Method: EM (helical sym.) / Resolution: 5.5 Å

3780

5ocu

EMDB-3780, PDB-5ocu:
Molecular basis of human kinesin-8 function and inhibition
Method: EM (helical sym.) / Resolution: 5.2 Å

3803

5ogc

EMDB-3803, PDB-5ogc:
Molecular basis of human kinesin-8 function and inhibition
Method: EM (helical sym.) / Resolution: 4.8 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

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

ChemComp-TA1:
TAXOL / medication, chemotherapy*YM

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-9V5:
4-chloranyl-2-nitro-1-(phenylsulfonyl)benzene

Source
  • bos taurus (cattle)
  • sus scrofa (pig)
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / Cytoskeleton / Motor protein / Kinesin

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