Handbook of Metalloproteins (VAP1: snake venom homolog of mammalian ADAMs) (book chapter, p.1-15) (DOI:10.1002/0470028637.met234)
Handbook of Metalloproteins (VAP1: snake venom homolog of mammalian ADAMs) (book chapter, p.1-15) (DOI:10.1002/0470028637.met234)
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金属蛋白手册（VAP1：哺乳动物 ADAM 的蛇毒同源物）（书籍章节，第 1-15 页）(DOI:10.1002/0470028637.met234)
DOI：
10.1002/0470028637.met234
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发表时间：
2008
期刊：
影响因子：
--
通讯作者：
Takeda S
中科院分区：
文献类型：
--
作者：
武田壮一;五十嵐智子;盛英三;Takeda S
血管凋亡诱导蛋白-1 (VAP1) 是来自西部小菜蛇Crotalus atroxvenom 的锌内肽酶。 VAP1 拥有金属蛋白酶/解整合素/富含半胱氨酸 (MDC) 结构域，该结构域具有 adamalysin/reprolysin/ADAM（解整合素和金属蛋白酶）蛋白质家族的典型结构域。哺乳动物 ADAM 蛋白酶的独特之处在于它们同时具有蛋白水解和粘附特性。此外，作为细胞表面蛋白，它们构成一类主要的膜锚定脱落酶，并参与细胞表面蛋白胞外域的加工，包括潜在形式的生长因子、细胞因子和受体。 VAP1的晶体结构揭示了C形MDC结构域结构以及C结构域中潜在的蛋白质-蛋白质相互作用位点，该位点面向M结构域中的催化位点。 VAP1 和相关蛋白的结构表明，adamalysin/reprolysin/ADAM 家族的蛋白酶中的蛋白水解和粘附功能之间存在相互作用。
Vascular‐apoptosis‐inducing protein‐1 (VAP1) is a zinc endopeptidase from western diamondback snakeCrotalus atroxvenom. VAP1 possesses a metalloproteinase/disintegrin/cysteine‐rich (MDC) domain that bears the typical domain architecture of the adamalysin/reprolysin/ADAM (a disintegrin and metalloproteinase) family of proteins. Mammalian ADAM proteinases are unique in that they have both proteolytic and adhesive properties. Additionally, as cell‐surface proteins, they constitute a major class of membrane‐anchored sheddases and participate in the processing of cell‐surface‐protein ectodomains, including the latent forms of growth factors, cytokines, and receptors. The crystal structures of VAP1 reveal a C‐shaped MDC domain architecture and a potential protein–protein interaction site in the C domain that faces the catalytic site in the M domain. The structures of VAP1 and related proteins suggest that there is interplay between proteolytic and adhesive functions in the proteinases of the adamalysin/reprolysin/ADAM family.