Fig. 2: Comparison of mouse TNF-humanTNFR1 complex with and without compound. | Nature Communications

Fig. 2: Comparison of mouse TNF-humanTNFR1 complex with and without compound.

From: Structural insights into the disruption of TNF-TNFR1 signalling by small molecules stabilising a distorted TNF

Fig. 2

Top view (a) and side view (b) of trimeric mTNF (green ribbons, monomers assigned A, B and C) with three copies of monomeric receptor-bound (pink surface rendered) (PDB: 7KP7 [https://www.rcsb.org/structure/unreleased/7KP7]). Top view (c) and side view (d) of trimeric mTNF (green ribbons) with UCB-4433 bound (orange space-fill) and two copies of dimeric hTNFR1 bound (pink and purple surface rendered) (PDB: 7KP8 [https://www.rcsb.org/structure/unreleased/7KP8]). e Side view of mTNF (green surface rendered) without compound—one copy of the hTNFR1 has been removed to reveal the non-distorted a–c receptor binding site (selected residues involved in hTNFR1 binding highlighted in red). f Side view of mTNF (green surface rendered) with UCB-4433 bound (not visible) revealing the distorted A–C receptor binding site (selected residues involved in receptor binding highlighted in red).

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