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PDBsum entry 2vwi
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237 a.a.
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264 a.a.
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271 a.a.
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References listed in PDB file
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Key reference
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Title
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Structure of the osr1 kinase, A hypertension drug target.
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Authors
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F.Villa,
M.Deak,
D.R.Alessi,
D.M.Van aalten.
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Ref.
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Proteins, 2008,
73,
1082-1087.
[DOI no: ]
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
perfect match.
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Abstract
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No abstract given.
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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).
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Figure 2.
Figure 2. OSR1 active conformation and conformational change
induced by RFXV peptide binding. (A) OSR1 activation segment
with the secondary structure elements and the residues discussed
in the text represented as cartoon and sticks, respectively,
colored in blue and red ( -strands
and -helices).
Shown in sticks are Lys46, Glu63, and Arg145. (B) CDK2
activation segment with the secondary structure elements and the
residues discussed in the text represented as cartoon and
sticks, respectively, colored in blue and red ( -strands
and -helices).
Shown in sticks are Lys33, Glu51, and Arg126. (C) Model of the
active conformation of the OSR1 kinase domain with the
activation segment and -helix
C represented as cartoon. Shown in sticks are Lys46, Glu63,
Arg145, Arg183, and Thr185. (D) Distance-distribution function
are for the OSR1(1-527) protein and for OSR1(1-527)-RFXV peptide
complex as determined by SAXS. Radius of gyration and D[max] are
also indicated. Vector length is shown as Å and p(r) as
arbitrary unit.
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The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2008,
73,
1082-1087)
copyright 2008.
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