The annexins.
The annexins.
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DOI：
10.1186/gb-2004-5-4-219
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发表时间：
2004
期刊：
影响因子：
12.3
通讯作者：
Morgan RO
中科院分区：
文献类型：
--
作者：
Moss SE;Morgan RO
膜联蛋白传统上被认为是钙依赖性磷脂结合蛋白，但最近的工作表明一组更复杂的功能。在主要的真核生物门中已经鉴定了超过一千种膜联蛋白超家族的蛋白质，但是膜联蛋白不存在于酵母和原核生物中。膜联蛋白传统上被认为是钙依赖性磷脂结合蛋白，但最近的工作表明一组更复杂的功能。在主要的真核生物门中已经鉴定了超过一千种膜联蛋白超家族的蛋白质，但是膜联蛋白不存在于酵母和原核生物中。独特的膜联蛋白核心结构域由四个相似的重复序列组成，长度约为70个氨基酸，每个重复序列通常含有一个特征性的“2型”基序，用于结合钙离子。动物和真菌膜联蛋白也具有不同长度和序列的非同源氨基末端结构域，其通过翻译后修饰和与其他蛋白质结合来负责蛋白质的独特定位和专门功能。膜联蛋白与各种细胞膜组分相互作用，这些组分参与细胞的结构组织、通过酶调节和离子通量的细胞内信号传导、生长控制，并且它们可以充当非典型钙通道。在核心结构域的位点特异性保护的分析表明，在脊椎动物膜联蛋白的钙通道活性和在其核心结构域的结构稳定性的某些掩埋的残基的作用。亚家族之间的进化显著差异优先定位于蛋白质表面上决定膜结合和与胞质蛋白相互作用的可接近位点。
Annexins are traditionally thought of as calcium-dependent phospholipid-binding proteins, but recent work suggests a more complex set of functions. More than a thousand proteins of the annexin superfamily have been identified in major eukaryotic phyla, but annexins are absent from yeasts and prokaryotes. Annexins are traditionally thought of as calcium-dependent phospholipid-binding proteins, but recent work suggests a more complex set of functions. More than a thousand proteins of the annexin superfamily have been identified in major eukaryotic phyla, but annexins are absent from yeasts and prokaryotes. The unique annexin core domain is made up of four similar repeats approximately 70 amino acids long, each of which usually contains a characteristic 'type 2' motif for binding calcium ions. Animal and fungal annexins also have non-homologous amino-terminal domains of varying length and sequence, which are responsible for the distinct localizations and specialized functions of the proteins through post-translational modification and binding to other proteins. Annexins interact with various cell-membrane components that are involved in the structural organization of the cell, intracellular signaling by enzyme modulation and ion fluxes, growth control, and they can act as atypical calcium channels. Analysis of site-specific conservation in the core domain suggests a role for certain buried residues in the calcium-channel activity of vertebrate annexins and in the structural stability of their core domains. Evolutionarily significant differences between subfamilies are preferentially localized to accessible sites on the protein surface that determine membrane binding and interactions with cytosolic proteins.
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影响因子：
5.8
作者：
Glaser, F;Pupko, T;Ben-Tal, N
通讯作者：
Ben-Tal, N
影响因子：
3
作者：
Schuster-Böckler, B;Schultz, J;Rahmann, S
通讯作者：
Rahmann, S
影响因子：
10.7
作者：
Gu, X
通讯作者：
Gu, X
影响因子：
5.3
作者：
Herr, C;Smyth, N;Noegel, AA
通讯作者：
Noegel, AA
影响因子：
64.5
作者：
HUANG, KS;WALLNER, BP;PEPINSKY, RB
通讯作者：
PEPINSKY, RB