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. Author manuscript; available in PMC: 2014 Aug 26.
Published in final edited form as: N Engl J Med. 2010 Jul 22;363(4):343–354. doi: 10.1056/NEJMoa0910500

Figure 5. Conformational Diversity and Differential Reactivity of α345 Noncollagenous-1 Hexamers of the Glomerular Basement Membrane.

Figure 5

The diagram shows a portion of the collagen IV network with the α345 noncollagenous-1 (NC1) hexamer tethered to the triple-helical domain. The different possible NC1 conformers shown are the cross-linked form stabilized by sulfilimine bonds (conformer 1 [C-1]), the non-cross-linked form (C-2), and the form in which the NC1 hexamers are dissociated into trimers (C-3). In Goodpasture’s disease the latter may undergo a conformational change resulting in the formation of neoepitopes shown as white squares on the α3NC1 (red) and α5NC1 (green) subunits of C-4, eliciting antibody formation and subsequent binding to conformers C-3 and C-4. Conformers C-1 and C-2 have the potential to be transformed into the pathogenic conformer C-4.