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. Author manuscript; available in PMC: 2017 Feb 20.
Published in final edited form as: Biochem J. 2016 Nov 22;474(3):385–398. doi: 10.1042/BCJ20160792

Figure 1. Proposed roles of the MARK1 KA1 domain.

Figure 1

The C-terminal KA1 domain (cyan) of MARK1 (PDB: 3OSE) is separated from the kinase (green) and UBA (orange) domains (PDB: 2HAK) by a linker of ~300 amino acids that is predicted to be unstructured [13, 15]. The KA1 domain has been separately implicated in autoinhibition of kinase activity [13], binding to anionic phospholipid membranes [12], and binding to Gab1 (not shown) [49]. Numbering is shown for human MARK1.