 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](va5008fig1mag.jpg)
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Figure 1
Structure of 2Apro from HRV-C15. (a) Overall structure of HRV-C15 2Apro chain B. The N-terminal domain and the C-terminal domain of HRV-C15 2Apro are shown in red and cyan, respectively. The zinc ion is represented as a magenta-coloured sphere. (b) The catalytic triad of HRV-C15 2Apro is located beneath the bII2–cII1 loop. The active-site residues are shown as sticks. (c) A tetrahedral coordination site for the zinc ion in the HRV-C15 2Apro structure. (d) The amino-acid sequences of 2Apro from human rhinovirus C15 (HRV-C15), human rhinovirus C2 (HRV-C2), human rhinovirus A2 (HRV-A2), coxsackievirus A16 (CVA16), human enterovirus 71 (EV71) and poliovirus 1 (Polio1) were aligned using ClustalW2 (Larkin et al., 2007  ), and the result of the alignment was graphically displayed using ESPript (Gouet et al., 1999). Secondary-structure elements are indicated according to the structure of 2Apro from HRV-C15. The red arrows show the conserved active site and the grey arrows show the Zn2+-binding site. |
![[Figure 1]](va5008fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
