Fig. 2: Stabilisation of Cμ2 domain in subunit 1. | Nature Communications

Fig. 2: Stabilisation of Cμ2 domain in subunit 1.

From: Cryomicroscopy reveals the structural basis for a flexible hinge motion in the immunoglobulin M pentamer

Fig. 2

a, b Zoomed-in view at threshold 0.6 of Cμ2-1 (red, pdb id 4JVU), Cμ3-1 A - Cμ4-1 A (cyan, pdb id 6KXS) and hairpin-3 of J-chain (dark blue) showing the relationships between the domains. The red dotted ellipse highlighting the interacting sections between J-chain and Cμ3-1 A. The black arrowheads in (b) point at the densities corresponding to N-linked glycosylation at N402 and N395 (densities of glycosylation are visible at all the other Cμ3 densities in Fig. 1a). c Overlay of the Cμ4-Cμ3 models of subunit 1 (cyan) and the rest of the subunits (subunit 2-5, light grey). The cyan arrows indicate the relative displacement of Cμ3-1 A.

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