Crystal structure of the catalytic domain of human ADAM33.

By P. Orth, P. Reichert, Wenyan Wang, W. Prosise, T. Yarosh-Tomaine, G. Hammond, Richard N. Ingram, Li Xiao, U. Mirza, Jun Zou and 4 more. 2004

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Accurate prediction of protein structures and interactions using a 3-track neural network (2021, neutral): “The ADAMs contain prodomain and metalloprotease domains; the fold of the metalloprotease isknown( 23 , 24 ),butthefoldoftheprodomain, which has no homologs of known structure, is not.”
The ADAM metalloproteinases (2008, background): “Thus although ADAM-17 and ADAM-33 (which to date are the only members of the mammalian ADAM family proper for which the structures have been solved) possess the same layout of secondary structure elements, their catalytic domains share only 26% identity (Orth et al., 2004).”
Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C‐shaped scaffold (2006, background): “A peptide-like hydroxamate inhibitor GM6001 binds to VAP1 (Figure 1A and B, and Supplementary Figure 2D and E) in exactly the same manner as in the marimastat-ADAM33 M-domain complex (Orth et al, 2004), suggesting that the catalytic sites of VAP1 and ADAM33 share a common substrate recognition mecha”
ADAM and ADAMTS Family Proteins and Snake Venom Metalloproteinases: A Structural Overview (2016, unknown): “ADAM8 human M 4DD8 2012 [68] ADAM10 bovine DC 2AO7 2005 [48] ADAM17 human M 1BKC 1998 [64] ADAM17 human C 2M2F (NMR) 2013 [69] ADAM22 human MDCE 3G5C 2009 [65] ADAM33 human M 1R54, 1R55 2004 [70]”