1. Volume 6, Issue 1, Pages 183-189 (July 2000)
Crystal Structure of Human Survivin Reveals a Bow Tie–Shaped Dimer with Two Unusual α-Helical Extensions 
Laurent Chantalat, Dimitrios A. Skoufias, Jean-Philippe Kleman, Barbara Jung, Otto Dideberg, Robert L. Margolis 
Molecular Cell 
Volume 6, Issue 1, Pages (July 2000)
DOI: /S (05)

2. Figure 1 Ribbon Representation of the Survivin Dimer
The β strands, α helices, and loops are represented as violet arrows, green coils, and brown lines, respectively. The zinc atoms are shown as blue spheres, and black arrows indicate the trypsin cleavage sites. Figures were drawn as described in Chantalat et al
(A) The dimer 2-fold axis is in the plane.
(B) The view in (A) rotated by 90° around the horizontal axis; the 2-fold axis is perpendicular to the plane.
Molecular Cell 2000 6, DOI: ( /S (05) )

3. Figure 2 Molecular Surface of the Survivin Dimer
Colored according to the local chemical properties: acidic, basic, polar, and hydrophobic are in red, blue, white, and yellow, respectively.
(A) The view is along the 2-fold axis going into the convex surface of the dimer.
(B) The view in (A) rotated by 90° around the horizontal axis.
(C) The view in (A) rotated by 180° around the horizontal axis. The 2-fold axis now going into the concave surface of the dimer.
Molecular Cell 2000 6, DOI: ( /S (05) )

4. Figure 3 Sequence Alignment of Survivin-Related Proteins
The figure shows alignment between human (hSURV) and mouse (mSURV) survivin, Drosophila deterin (dDETER), and two IAP domains of known 3D structure (residues 255–352 of MIHB and residues 149–240 of XIAP; GenBank accession numbers: hSURV, U75285; mSURV, AF115517; dDETER, AI260030; MIHB, U37547; and XIAP, U32974). The secondary structural elements for human survivin are indicated above the alignment. Conserved residues in the zinc finger domain are boxed in red. The BIR domain and zinc ligands are underlined with horizontal stripes in blue and yellow, respectively. The trypsin cleavage site is marked by a black arrow.
Molecular Cell 2000 6, DOI: ( /S (05) )

5. Figure 4
Structure Conservation of the Zinc Finger Domain and Detail of the Dimer Interface
(A) Superimposition of two zinc finger domains, MIHB (G263–G341 in cyan) and survivin (T5-E94 in green), shown in stereo view. For clarity, only the zinc ligands (cysteines in yellow and histidine in deep blue) and the zinc ion (light blue) of survivin are represented. The two conserved arginines (R272 and R18 of MIHB and survivin, respectively) are shown color coded as the main chain. The two conserved glycines (G294 and G42 of MIHB and survivin, respectively) are also marked.
(B) Ribbon stereo view of the dimer interface. The α helices are shown as green coils and loops as brown lines. Amino acid side chains involved in protein–protein interactions are represented in ball-and-stick in black. Hydrogen bonds are shown as dotted red lines.
(C) The various contacts at the dimer interface are displayed as a schematic diagram. Hydrogen bonds and van der Waals interactions are indicated by black arrows (donor to acceptor) and blue lines, respectively.
Molecular Cell 2000 6, DOI: ( /S (05) )