In:
Protein Science, Wiley, Vol. 15, No. 11 ( 2006-11), p. 2534-2543
Abstract:
Microtubule‐associated protein/microtubule affinity‐regulating kinases (MARKs)/PAR‐1 are common regulators of cell polarity that are conserved from nematode to human. All of these kinases have a highly conserved C‐terminal domain, which is termed the kinase‐associated domain 1 (KA1), although its function is unknown. In this study, we determined the solution structure of the KA1 domain of mouse MARK3 by NMR spectroscopy. We found that ∼50 additional residues preceding the previously defined KA1 domain are required for its proper folding. The newly defined KA1 domain adopts a compact α+β structure with a βαββββα topology. We also found a characteristic hydrophobic, concave surface surrounded by positively charged residues. This concave surface includes the highly conserved Glu‐Leu‐Lys‐Leu motif at the C terminus, indicating that it is important for the function of the KA1 domain.
Type of Medium:
Online Resource
ISSN:
0961-8368
,
1469-896X
DOI:
10.1110/ps.062391106
Language:
English
Publisher:
Wiley
Publication Date:
2006
detail.hit.zdb_id:
2000025-X
SSG:
12
Permalink