PDBsum entry 4fdd

Transport protein

PDB id: 4fdd

Contents

Protein chains

836 a.a.

20 a.a.

Waters ×148

References listed in PDB file

Key reference

Title

Structural and energetic basis of als-Causing mutations in the atypical proline-Tyrosine nuclear localization signal of the fused in sarcoma protein (fus).

Authors

Z.C.Zhang, Y.M.Chook.

Ref.

Proc Natl Acad Sci U S A, 2012, 109, 12017-12021.

PubMed id

22778397

Abstract

No abstract given.

Secondary reference #1

Title

Conformational heterogeneity of karyopherin beta2 is segmental.

Authors

A.E.Cansizoglu, Y.M.Chook.

Ref.

Structure, 2007, 15, 1431-1441. [DOI no: 10.1016/j.str.2007.09.009]

PubMed id

17997969

Figure 3.
Figure 3. Hinge Motion in the C-Terminal Arch of Kapβ2
Stereo diagrams of the C-terminal arch (H9–H20) of chains A–D of unliganded Kapβ2 and substrate- and Ran-bound Kapβ2s superimposed at H9–H13 and drawn as spheres at the geometric center of each HEAT repeat. The hinge axes that rotate unliganded Kapβ2 with respect to substrate- and Ran-bound Kapβ2s are in pink and red, respectively.

Figure 4.
Figure 4. Conformational Change in the Kapβ2 N-Terminal Arch
(A) Ribbon diagram of the N-terminal arches of chains A (blue) and C (light blue) of unliganded Kapβ2, superimposed at H9–H13.
(B) Same as (A), except that chain A of unliganded Kapβ2 is superimposed on substrate-bound Kapβ2 (pink).
(C) Same as (A), except that chain A of Kapβ2 is superimposed on Ran-bound Kapβ2 (red). Ran is shown as a surface representation in gray and the H8 loop of the Ran complex is in yellow.

The above figures are reproduced from the cited reference with permission from Cell Press

Secondary reference #2

Title

Structure-Based design of a pathway-Specific nuclear inhibitor.

Authors

A.E.Cansizoglu, B.J.Lee, Z.C.Zhang, B.M.Fontoura, Y.M cho.

Ref.

nat struct mol biol, 2007, 14, 452.

Secondary reference #3

Title

Rules for nuclear localization sequence recognition by karyopherin beta 2.

Authors

B.J.Lee, A.E.Cansizoglu, K.E.Süel, T.H.Louis, Z.Zhang, Y.M.Chook.

Ref.

Cell, 2006, 126, 543-558. [DOI no: 10.1016/j.cell.2006.05.049]

PubMed id

16901787

Figure 1.
Figure 1. Crystal Structure of the Kapβ2-M9NLS Complex

Figure 3.
Figure 3. Consensus Sequences of NLSs Recognized by Kapβ2

The above figures are reproduced from the cited reference with permission from Cell Press

Secondary reference #4

Title

Structure of the nuclear transport complex karyopherin-Beta2-Ran x gppnhp.

Authors

Y.M.Chook, G.Blobel.

Ref.

Nature, 1999, 399, 230-237. [DOI no: 10.1038/20375]

PubMed id

10353245

Figure 1.
Figure 1: Stereoview of a ribbon drawing of Kap- beta-2 bound to Ran bullet-GppNHp. Kap- 2 is orange and residues 311–373 (L7) are highlighted in yellow to emphasize its deviation from the HEAT repeat structure and its displacement from the main bodyof the protein. Ran is blue; the nucleotide analogue GppNHp is depicted with ball-and-stick representation and Mg^2+ is a white sphere. Ribbon diagrams were generated using MOLSCRIPT^48 and RASTER3D^49.

Figure 5.
Figure 5: Kap- beta-2–Ran and RBD1–Ran interfaces are mostly non-overlapping but adjacent in the Ran structure. RBD1 may be able to access Ran through the opening of the N-terminal arch. Kap- 2–Ran GppNHp complex is shown with the N-terminal arch of Kap- 2 lying on the horizontal plane, with an oblique view into the opening of the arch. The colour scheme is similar to Fig. 4a , with the addition of residues on Ran interacting with RBD1 (ref. 23) coloured purple and the Ran C-terminal extension in cyan. Side chains of N154 and E158 in Ran are purple while their main chains are green, as these residues interact with both Kap- 2 and RBD1.

The above figures are reproduced from the cited reference with permission from Macmillan Publishers Ltd