 |
PDBsum entry 1bk6
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Complex (protein transport/peptide)
|
PDB id
|
|
|
|
1bk6
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha.
|
|
|
Authors
|
|
E.Conti,
M.Uy,
L.Leighton,
G.Blobel,
J.Kuriyan.
|
|
|
Ref.
|
|
Cell, 1998,
94,
193-204.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Selective nuclear import is mediated by nuclear localization signals (NLSs) and
cognate transport factors known as karyopherins or importins. Karyopherin alpha
recognizes "classical" monopartite and bipartite NLSs. We report the
crystal structure of a 50 kDa fragment of the 60 kDa yeast karyopherin alpha, in
the absence and presence of a monopartite NLS peptide at 2.2 A and 2.8 A
resolution, respectively. The structure shows a tandem array of ten armadillo
repeats, organized in a right-handed superhelix of helices. Binding of the NLS
peptide occurs at two sites within a helical surface groove that is lined by
conserved residues. The structure reveals the determinants of NLS specificity
and suggests a model for the recognition of bipartite NLSs.
|
|
|
|
|
|
|
|
Figure 2.
Figure 2. Three-Dimensional Structure of Kapα50The molecule
contains ten tandem arm repeats, which are shown in different
colors. With the exception of the first motif, each arm repeat
includes three α helices (H1, H2, and H3). The superhelical
axis of the molecule is vertical. All ribbon diagrams were
generated using RIBBONS ([6]).
|
|
Figure 6.
Figure 6. The Kapα50 Dimer in the Crystals(A) Dimer of
Kapα50 viewed approximately down the local molecular dyad axis,
with the two monomers colored in green and magenta. The arm
repeats are numbered sequentially from the N to the C terminus.
The helices of the tenth arm motifs are labeled. Note that the
first arm repeat lacks the H1 helix.(B) The dimer interactions
between the tenth arm repeat of one monomer (in gray with
relevant residues depicted in magenta) contacting the H3 helices
of the central repeats of the second monomer (in gray with
important residues highlighted in green). All the labeled side
chains are highly conserved. Hydrogen bonding contacts are shown
in dotted lines.
|
|
|
|
|
|
The above figures are
reprinted
by permission from Cell Press:
Cell
(1998,
94,
193-204)
copyright 1998.
|
|
|
|
|
|
|
