Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C‐shaped scaffold

By S. Takeda, T. Igarashi, H. Mori, S. Araki. 2006

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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.”
A Disintegrin and Metalloproteinase (ADAM) and ADAM with Thrombospondin Motifs (ADAMTS) Family in Vascular Biology and Disease (2019, background): “The discovery of the C-shape scaffold, was a landmark study in deciphering the crystal structure of ADAMs and how they function [9].”
A Disintegrin and Metalloprotease (ADAM): Historical Overview of Their Functions (2016, background): “In addition to mediating interactions with cell surface receptors for adhesive and fusogenic purposes, the disintegrin and cysteine domains were suggested to regulate the proteolytic function of ADAMs as shown for the shedding of interleukin-1 receptor-II by ADAM-17 [19].”
ADAMs family and relatives in cardiovascular physiology and pathology. (2016, background): “Modified from [15].”
The ADAM metalloproteinases (2008, background): “(2006) .”
ADAM and ADAMTS Family Proteins and Snake Venom Metalloproteinases: A Structural Overview (2016, background): “In ADAMs and P-III SVMPs, the RGD sequence is usually replaced by an (D/S)XCD sequence (residues 466–469 in the catrocollastatin/VAP2B sequence).”