Secondary structure of neutrophil-activating peptide-2 determined by 1H-nuclear magnetic resonance spectroscopy.
Secondary structure of neutrophil-activating peptide-2 determined by 1H-nuclear magnetic resonance spectroscopy.
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通过 1H 核磁共振波谱测定中性粒细胞激活肽-2 的二级结构。
DOI：
10.1042/bj3040371
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发表时间：
1994
期刊：
影响因子：
--
通讯作者：
LaRosa,GJ
中科院分区：
文献类型：
--
作者：
Mayo,KH;Yang,Y;Daly,TJ;Barry,JK;LaRosa,GJ
中性粒细胞激活蛋白-2(NAP-2)是一种由72个氨基酸残基组成的蛋白，具有多种促炎活性。用二维1H-n.m.r研究了单体NAP-2的溶液结构。光谱学。根据原子核Overhauser数据、耦合常数和酰胺氢/氚交换，进行了特定序列的质子共振指认，并确定了二级结构元素。NAP-2单体由以希腊键和C末端螺旋(残基59-70)排列的三链反平行β-折叠组成，与n.m.r中发现的非常相似。二聚体白介素8的溶液构象和四聚体牛血小板因子-4的晶体结构。根据肝素结合和NAP-2的中性粒细胞激活特性对结果进行了讨论。
Neutrophil-activating protein-2 (NAP-2) is a 72 residue protein demonstrating a range of proinflammatory activities. The solution structure of monomeric NAP-2 has been investigated by two-dimensional 1H-n.m.r. spectroscopy. Sequence-specific proton resonance assignments have been made and secondary structural elements have been identified on the basis of nuclear Overhauser data, coupling constants and amide hydrogen/deuteron exchange. The NAP-2 monomer consists of a triple-stranded anti-parallel beta-sheet arranged in a ‘Greek key’ and a C-terminal helix (residues 59-70) and is very similar to that found in the n.m.r. solution conformation of dimeric interleukin-8 and the crystal structure of tetrameric bovine platelet factor-4. Results are discussed in terms of heparin binding and neutrophil-activation properties of NAP-2.