Figure 1.
Figure 1. Overall structure of the OSR1 kinase domain. (A)
Multiple sequence alignment of human OSR1 and SPAK kinases and
some members of the STE group previously crystallized (TAO2,
PAK1, and PAK4). Secondary structure elements and numbering are
according to human OSR1. TAO2, PAK1, and PAK4 sequences
correspond to the protein crystallized and deposited in the PDB
database (PDB codes 1U5R, 1YHV, and 2BVA, respectively). The
threonine (Thr185) targeted by WNK is labelled with a red star
and Arg183 with a green circle. (B) Cartoon representation of
the OSR1 kinase domain, colored in blue and red ( -strands
and -helices,
respectively) apart for -helix
L[12] (yellow). The secondary structure elements are labeled in
agreement with [Fig. 1(A)]. The AMP-PNP molecule in the OSR1
active site is represented as sticks (magenta) with an unbiased
Fo-Fc electron density map (green), ( level
= 2.5). (C) Domain-exchanged kinase dimer. The activation
segment from each monomer extends to form an extensive
intermolecular interface. Molecular surface (yellow) is shown
for one monomer, while the other monomer is shown as a cartoon.
The disordered activation segment is represented as dotted lines
and bound nucleotide is shown as stick (magenta).
The above figure is reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2008,
73,
1082-1087)
copyright 2008.
-strands
and 
-helices,
respectively) apart for 
level
= 2.5). (C) Domain-exchanged kinase dimer. The activation
segment from each monomer extends to form an extensive
intermolecular interface. Molecular surface (yellow) is shown
for one monomer, while the other monomer is shown as a cartoon.
The disordered activation segment is represented as dotted lines
and bound nucleotide is shown as stick (magenta).