1zmv
Catalytic and ubiqutin-associated domains of MARK2/PAR-1: K82R mutant
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OverviewOverview
The Ser/Thr kinase MARK2 phosphorylates tau protein at sites that cause, detachment from microtubules in Alzheimer neurofibrillary degeneration., Homologs of MARK2 include Par-1 in C. elegans and Drosophila, which, generates embryonic polarity. We report the X-ray structure of the, catalytic and ubiquitin-associated domains (UBA) of human MARK2. The, activity was altered by mutations in the ATP binding site and/or, activation loop. The catalytic domain shows the small and large lobes, typical of kinases. The substrate cleft is in an inactive, open, conformation in the inactivated and the wild-type structure. The UBA, domain is attached via a taut linker to the large lobe of the kinase, domain and leans against a hydrophobic patch on the small lobe. The UBA, structure is unusual because the orientation of its third helix is, inverted, relative to previous structures. Possible implications of the, structure for the regulation of kinase activity are discussed.
About this StructureAbout this Structure
1ZMV is a Single protein structure of sequence from Rattus norvegicus. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
ReferenceReference
Structure of the catalytic and ubiquitin-associated domains of the protein kinase MARK/Par-1., Panneerselvam S, Marx A, Mandelkow EM, Mandelkow E, Structure. 2006 Feb;14(2):173-83. PMID:16472737
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