Backbone and side-chain (1)H, (13)C and (15)N resonance assignments of LEN, a human immunoglobulin kappaIV light-chain variable domain.
Backbone and side-chain (1)H, (13)C and (15)N resonance assignments of LEN, a human immunoglobulin kappaIV light-chain variable domain.
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LEN（人免疫球蛋白 kappaIV 轻链可变域）的主链和侧链 (1)H、(13)C 和 (15)N 共振分配。
DOI：
10.1007/s12104-009-9188-y
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发表时间：
2009
影响因子：
0.9
通讯作者：
Jaroniec,ChristopherP
中科院分区：
文献类型：
--
作者：
Mukherjee,Sujoy;Pondaven,SimonP;Höfer,Nicole;Jaroniec,ChristopherP
重组的114个氨基酸的人免疫球蛋白(Ig) κIV轻链可变结构域（VL） LEN与另一个人免疫球蛋白κIV轻链可变结构域SMA具有高度的序列同源性。SMA在体内和体外都是高度淀粉样变性的，并且与轻链淀粉样变性的发病机制有关，而LEN在体内是非淀粉样变性的，只有在体外不稳定条件下才能转化为淀粉样状态。纵向和横向酰胺15n弛豫率的测量证实，正如预期的那样，LEN在生理pH值和核磁共振研究的典型浓度下是二聚体，次级化学位移分析表明该蛋白具有高β-片含量。这些发现与先前发表的生物物理数据和LEN的高分辨率x射线结构一致。
1H,13C and15N resonance assignments are presented for a recombinant 114 amino acid human immunoglobulin (Ig) κIV light-chain variable domain (VL) LEN, which displays a high degree of sequence identity with another human Ig κIV VL, SMA. While SMA is highly amyloidogenic in vivo and in vitro and has been linked to the pathogenesis of light-chain amyloidosis, LEN is non-amyloidogenic in vivo and can be converted to the amyloid state only in vitro under destabilizing conditions. Measurements of longitudinal and transverse amide15N relaxation rates confirm that, as expected, LEN is a dimer at physiological pH and typical concentrations used for NMR studies, and the analysis of secondary chemical shifts indicates that the protein has a high β-sheet content. These findings are consistent with previously published biophysical data and the high-resolution X-ray structure of LEN.