 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 2]](mn5037fig2mag.jpg)
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Figure 2
Stoichiometry and trimeric interface of the structure of the TRAF4 TRAF domain with a coiled-coil domain. (a) Gel-filtration chromatography profile. (b) Multi-angle light scattering (MALS) results. The red line indicates the experimental molecular weight. (c) The trimeric structure of the TRAF4 TRAF domain with a coiled-coil domain. A close-up of the interacting residues in the interface between two monomeric TRAF4 TRAF domains with a coiled-coil domain (blue for chain A and yellow for chain B) is shown on the right. The residues involved in the contact are shown. The salt bridge formed between Glu291 from one chain and Gln293 from its counterpart is shown as a red dashed line. Hydrogen bonds are shown as black dashed lines. |
![[Figure 2]](mn5037fig2.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
