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Protein Minimization of the gp120 Binding Region of Human CD4

机译：人CD4的GP120结合区的蛋白质最小化

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CD4 is an important component of the immune system and is also the cellular receptor for HIV-1.CD4 consists of a cytoplasmic tail,one transmembrane region,and four extracellular domains,D1-D4.Constructs consisting of all four extracellular domains of human CD4 as well as the first two domains(CD4D12)have previously been expressed and characterized.All of the gp120-binding residues are located within the first N-terminal domain(D1)of CD4.To date,it has not been possible to obtain domain D1 alone in a soluble and active form.Most residues in CD4 that interact with gp120 lie within the region 21-64 of domain D1 of CD4.On the basis of these observations and analysis of the crystal structure of CD4D12,a mutational strategy was designed to express CD4D1 and region 21-64 of CD4(CD4PEP1)in Escherichia coli.K_D values for the binding of CD4 analogues described above to gp120 were measured using a Biacore-based solution-phase competition binding assay.Measured K_D values were 15 nM,40 nM,and 26 muM for CD4D12,CD4D1,and CD4PEP1,respectively.All of the proteins interact with gp120 and are able to expose the 17b-binding epitope of gp120.Structural content was determined using CD and proteolysis.Both CD4D1 and CD4PEP1 were partially structured and showed an enhanced structure in the presence of the osmolyte sarcosine.The aggregation behavior of all of the proteins was characterized.While CD4D1 and CD4PEP1 did not aggregate,CD4D12 formed amyloid fibrils at neutral pH within a week at 278 K.These CD4 derivatives should be useful tools in HIV vaccine design and entry inhibition studies.
机译：CD4是免疫系统的重要组成部分，也是HIV-1.CD4的细胞受体由细胞质尾，一个跨膜区和四个细胞外结构域D1-D4。构成由所有四个人CD4的细胞外域组成。以及先前已经表达并表达了前两个域（CD4D12）。GP120结合残基的所有末端都位于CD4的第一n末端域（D1）内。迄今为止，还没有获得域D1单独以溶于溶于和活性的形式。在CD4的结构域D1的区域21-64中相互作用的CD4中的各个残基在CD4D12的晶体结构的基础上，设计了一种突变策略的基础。为了表达在大肠杆菌的CD4（CD4Pep1）的CD4D1和CD4（CD4Pep1）的CD4D1和区域21-64，用于使用基于Biacore的溶液相竞争结合测定测量上述CD4类似物的CD4类似物的值。Q_D值为15nm， 40 nm，26分别为CD4D12，CD4D1和CD4Pep1的妈妈。所有蛋白质与GP120相互作用，并且能够暴露GP120的17b结合表位。使用Cd和蛋白水解测定结构含量。结束CD4D1和CD4Pep1部分地构造并显示出一个在渗透肌肉肌氨酸存在下增强结构。所有蛋白质的聚集行为都表征。CD4D1和CD4Pep1没有聚集，CD4D12在278k的一周内在中性pH下在中性pH下形成淀粉样蛋白原纤维。该CD4衍生物应该是有用的工具在艾滋病毒疫苗设计和进入抑制研究中。

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  • 来源
    《Biochemistry》 |2005年第49期|共11页
  • 作者

    Deepak Sharma; M.M.Balamurali; Kausik Chakraborty; Sowmini Kumaran; Sadasivam Jeganathan;

  • 作者单位

    Molecular Biophysics Unit Indian Institute of Science Bangalore 560 012 India and Istituto di Ricerche di Biologia Molecolare P.Angeletti Via Pontina Km 30.600 00040 Pomezia Italy;

    Molecular Biophysics Unit Indian Institute of Science Bangalore 560 012 India and Istituto di Ricerche di Biologia Molecolare P.Angeletti Via Pontina Km 30.600 00040 Pomezia Italy;

    Molecular Biophysics Unit Indian Institute of Science Bangalore 560 012 India and Istituto di Ricerche di Biologia Molecolare P.Angeletti Via Pontina Km 30.600 00040 Pomezia Italy;

    Molecular Biophysics Unit Indian Institute of Science Bangalore 560 012 India and Istituto di Ricerche di Biologia Molecolare P.Angeletti Via Pontina Km 30.600 00040 Pomezia Italy;

    Molecular Biophysics Unit Indian Institute of Science Bangalore 560 012 India and Istituto di Ricerche di Biologia Molecolare P.Angeletti Via Pontina Km 30.600 00040 Pomezia Italy;

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  • 正文语种 eng
  • 中图分类 生物化学;
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