文献詳細
文献概要
今月の特集2 ADAMTS13と臨床検査
ADAM/ADAMTSファミリープロテアーゼの構造と機能
著者: 武田壮一1
所属機関: 1国立循環器病研究センター研究所心臓生理機能部
ページ範囲:P.534 - P.540
文献購入ページに移動■ADAM/ADAMTSファミリーは特徴的なドメインがつながったモジュラー構造をもつプロテアーゼであり,触媒ドメインとともにエキソサイトドメインも,標的となる蛋白質分子の認識に重要な役割を担っている.
参考文献
1)Blobel CP, Wolfsberg TG, Turck CW, et al:A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature 356:248-252,1992
2)Wolfsberg TG, Straight PD, Gerena RL, et al:ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain. Dev Biol 169:378-383,1995
3)Black RA, Rauch CT, Kozlosky CJ, et al:A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells. Nature 385:729-733,1997
4)Moss ML, Jin SL, Milla ME, et al:Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α. Nature 385:733-736,1997
5)Edwards DR, Handsley MM, Pennington CJ:The ADAM metalloproteinases. Mol Aspects Med 29:258-289,2008
6)Fox JW, Serrano SM:Timeline of key events in snake venom metalloproteinase research. J Proteomics 72:200-209,2009
7)Kuno K, Kanada N, Nakashima E, et al:Molecular cloning of a gene encoding a new type of metalloproteinase-disintegrin family protein with thrombospondin motifs as an inflammation associated gene. J Biol Chem 272:556-562,1997
8)Apte SS:A disintegrin-like and metalloprotease (reprolysin-type) with thrombospondin type 1 motif (ADAMTS) superfamily:functions and mechanisms. J Biol Chem 284:31493-31497,2009
9)Takeda S, Takeya H, Iwanaga S:Snake venom metalloproteinases:structure, function and relevance to the mammalian ADAM/ADAMTS family proteins. Biochim Biophys Acta 1824:164-176,2012
10)Takeda S, Igarashi T, Mori H, et al:Crystal structures of VAP1 reveal ADAMs’ MDC domain architecture and its unique C-shaped scaffold. EMBO J 25:2388-2396,2006
11)Takeda S:Three-dimensional domain architecture of the ADAM family proteinases. Semin Cell Dev Biol 20:146-152,2009
12)Gerhardt S, Hassall G, Hawtin P, et al:Crystal structures of human ADAMTS-1 reveal a conserved catalytic domain and a disintegrin-like domain with a fold homologous to cysteine-rich domains. J Mol Biol 373:891-902,2007
13)Mosyak L, Georgiadis K, Shane T, et al:Crystal structures of the two major aggrecan degrading enzymes, ADAMTS4 and ADAMTS5. Protein Sci 17:16-21,2008
14)Akiyama M, Takeda S, Kokame K, et al:Crystal structures of the noncatalytic domains of ADAMTS13 reveal multiple discontinuous exosites for von Willebrand factor. Proc Natl Acad Sci U S A 106:19274-19279,2009
15)Zhang Q, Zhou YF, Zhang CZ, et al:Structural specializations of A2, a force-sensing domain in the ultralarge vascular protein von Willebrand factor. Proc Natl Acad Sci U S A 106:9226-9231,2009
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