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Sci. STKE, 28 August 2007
[DOI: 10.1126/stke.4012007re6]

Structure and Function of the PB1 Domain, a Protein-Interaction Module Conserved in Animals, Fungi, Amoebas, and Plants (Interactive Structures)

Hideki Sumimoto 1,2*, Sachiko Kamakura1,2 and Takashi Ito 2,3

1Medical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan. 2 CREST, Japan Science and Technology Agency, 5-3 Sanbancho, Chiyoda-ku, Tokyo 102-0075, Japan. 3 Department of Computational Biology, Graduate School of Frontier Sciences, University of Tokyo, 5-1-5 Kashiwanoha, Kashiwa 277-8561, Japan.

*Corresponding author. E-mail, hsumi{at}bioreg.kyushu-u.ac.jp

Interactive image 1. The Cdc24 PB1 domain. This structure is based on PDB entry 1Q1O and visualized with JMOL (1). The β-strands and α-helices are shown in yellow and green, respectively. This is an interactive version of the molecular structure shown in Figure 3. The static image to the right is the same one that appears in the full text of the review. In the static figure, the OPCA motif is highlighted in light blue. Conserved acidic residues in the OPCA motif are shown in stick representation and labeled in pink (static figure) or red (interactive figure).

Interactive image 2. Full-length p40phox. This structure is based on PDB entry 2DYB and visualized with JMOL (1). The β-strands and α-helices are shown in gold and pink, respectively. This is an interactive representation of the molecular structure shown in Figure 6. The static image to the right is the same one that appears in the full text of the review. In this case, the PX, SH3, and PB1 domains are shown in cyan, yellow, and magenta, respectively. The OPCA motif is highlighted in red.

Interactive image 3. The p40phox-p67phox PB1 complex. This structure is based on PDB entry 1OEY and visualized with JMOL (1). This is an interactive version of one of the molecular structures shown Figure 4. The static image to the right is the same one that appears in the full text of the review. The β strands and α helices are shown in yellow and green, respectively. The notations of these secondary structural elements are indicated (in the static view only). Conserved acidic residues in the OPCA motif of p40phox are highlighted as red sticks (and labeled in the static view). Basic residues of p67phox that interact with acidic residues of the OPCA motif are highlighted as blue sticks (and labeled in the static view).

Interactive image 4. The PKCι/λ-Par6α PB1 complex. This structure is based on PDB entry 1WMH and visualized with JMOL (1). The β-strands and α-helices are shown in yellow and green, respectively. This is an interactive version of one of the molecular structures shown Figure 4. The static image to the right is the same as the one that appears in the full text of the review. In the static view, the notations of these secondary structural elements are indicated, conserved acidic residues in the OPCA motif of PKCι/λ are highlighted as red sticks and labeled, and basic residues Par6α that interact with acidic residues of the OPCA motif are highlighted as blue sticks and labeled.

Tips for using the JMOL applet (1). To move the image, click in the image and hold the mouse button down and move the mouse. To zoom in or out, click in the image and hold down the mouse button with the "Shift" key depressed. In Windows, right-clicking anywhere on the JMOL image, or using either mouse button to click on the "JMOL" in the lower right corner will generate a pop-up menu that provides many options for changing the view. To restore the original view, reload the page in the browser. Please note that you may need to move the JMOL interactive versions of the images to orient them the same as the static images.

Reference

  1. Jmol: an open-source Java viewer for chemical structures in 3D. http://www.jmol.org/

Citation: H. Sumimoto, S. Kamakura, T. Ito, Structure and function of the PB1 domain, a protein-interaction module conserved in animals, fungi, amoebas, and plants. Sci. STKE 2007, re6 (2007).


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