 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 3]](nq5001fig3mag.jpg)
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Figure 3
Crystal structure of the TRIM21–suramin complex. (a) Surface representation of mouse TRIM21 (grey) complexed with suramin (pink). For orientation, the binding site of the antibody Fc region (blue) is shown based on PDB entry 3zo0. The position of the N-terminal His-tag is indicated. (b) 2Fo − Fc electron-density map for suramin, contoured at 1σ (blue mesh). (c) Electrostatic surface-charge representation of TRIM21. The His-tag has been removed in this panel for a clearer view of the ligand and its artificial nature. Even without the tag this area remains positively charged. (d) Suramin binding to TRIM21. Hydrogen bonds and ionic interactions between positively charged histidine residues and negatively charged sulfonate groups are shown as green dashed lines and π interactions are shown as black dashed lines. Noncanonical residues from the His-tag are prefixed with a minus sign. (e) Comparison of residues within 5 Å of suramin between mouse (grey) and human (blue) TRIM21. The tag residues are removed in this panel. |
![[Figure 3]](nq5001fig3.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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