The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form.
The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form.
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DOI：
10.1021/bi802175a
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发表时间：
2009-03-17
期刊：
影响因子：
2.9
通讯作者：
Evans, John Spencer
中科院分区：
文献类型：
--
作者：
Delak, Katya;Harcup, Craig;Lakshminarayanan, Rajamani;Sun, Zhi;Fan, Yuwwei;Moradian-Oldak, Janet;Evans, John Spencer
淀粉原蛋白是一类与脊椎动物矿化牙釉质形成相关的蛋白质，具有高度保守的N端和c端序列区域，是理解生物矿化和蛋白质组装的一个有趣的模型蛋白质系统。利用生物信息学，我们在此报告了将12种淀粉原蛋白分类为内在无序或非结构蛋白家族（IDPs）成员的分子特征的鉴定，这组蛋白质通常以未展开的物种存在，但能够转化为折叠状态，作为其整体功能的一部分。利用生物物理技术（CD和NMR），我们跟踪了我们的生物信息学研究，并证实其中一种淀粉原蛋白重组猪rP172以延伸的、未折叠的单体形式存在。该蛋白表现出两种状态之间的构象交换的证据，这种交换可能是由序列中的Pro残基介导的。虽然该蛋白是全局展开的，但我们检测到局部残余二级结构[α-螺旋，延伸β-链，转/环和聚脯氨酸II型（PPII）]的存在，这些结构可能在牙釉质基质中发挥多种功能作用。rP172淀粉原蛋白延伸的、不稳定的构象与淀粉原蛋白在牙釉质生物矿化中的已知功能是相容的，即自组装、与其他牙釉质基质蛋白和磷酸钙生物矿物的结合以及与细胞受体的相互作用。这种蛋白质的不稳定结构很可能促进了淀粉原蛋白与其他大分子或矿物质的相互作用，以实现内部蛋白质的稳定。
Amelogenins make up a class of proteins associated with the formation of mineralized enamel in vertebrates, possess highly conserved N- and C-terminal sequence regions, and represent an interesting model protein system for understanding biomineralization and protein assembly. Using bioinformatics, we report here the identification of molecular traits that classify 12 amelogenin proteins as members of the intrinsically disordered or unstructured protein family (IDPs), a group of proteins that normally exist as unfolded species but are capable of transformation to a folded state as part of their overall function. Using biophysical techniques (CD and NMR), we follow up on our bioinformatics studies and confirm that one of the amelogenins, recombinant porcine rP172, exists in an extended, unfolded state in the monomeric form. This protein exhibits evidence of conformational exchange between two states, and this exchange may be mediated by Pro residues in the sequence. Although the protein is globally unfolded, we detect the presence of local residual secondary structure [α-helix, extended β-strand, turn/loop, and polyproline type II (PPII)] that may serve several functional roles within the enamel matrix. The extended, labile conformation of rP172 amelogenin is compatible with the known functions of amelogenin in enamel biomineralization, i.e., self-assembly, associations with other enamel matrix proteins and with calcium phosphate biominerals, and interaction with cell receptors. It is likely that the labile structure of this protein facilitates interactions of amelogenin with other macromolecules or with minerals for achievement of internal protein stabilization.
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影响因子：
3.9
作者：
Kulp, JL;Shiba, K;Evans, JS
通讯作者：
Evans, JS
影响因子：
3.4
作者：
Li, Minfen;Liu, Jingxian;Song, Jianxing
通讯作者：
Song, Jianxing
影响因子：
2.9
作者：
Cubellis, MV;Caillez, F;Lovell, SC
通讯作者：
Lovell, SC
影响因子：
3
作者：
FINCHAM, AG;MORADIANOLDAK, J;SLAVKIN, HC
通讯作者：
SLAVKIN, HC
DOI：
10.1006/bbrc.1993.2468
发表时间：
1993-11-30
影响因子：
3.1
作者：
FINCHAM, AG;MORADIANOLDAK, J
通讯作者：
MORADIANOLDAK, J