Partial high-resolution structure of phosphorylated and non-phosphorylated leucine-rich amelogenin protein adsorbed to hydroxyapatite.
Partial high-resolution structure of phosphorylated and non-phosphorylated leucine-rich amelogenin protein adsorbed to hydroxyapatite.
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DOI：
10.1021/jp202965h
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发表时间：
2011-07-21
影响因子：
3.7
通讯作者：
Shaw, Wendy J.
中科院分区：
文献类型：
--
作者：
Masica, David L.;Gray, Jeffrey J.;Shaw, Wendy J.
生物质的形成需要有机分子与矿物相的相互作用。在形成牙釉质的过程中，釉原蛋白有助于羟基磷灰石(HAP)的矿化。富含亮氨酸的釉原蛋白(LRAP)是釉原蛋白的一种天然剪接变异体，它包含釉原蛋白预测的HAP结合域。我们使用结合固态核磁共振(SsNMR)和偏向计算结构预测的方法确定了与HAP结合的磷酸化和非磷酸化LRAP变体的部分结构。N-末端的新的ss核磁共振测量表明这两个变体都有很大程度的延伸结构，尽管一些测量结果与部分螺旋的N-末端片段一致。发现磷酸化变异体的N-末端始终比非磷酸化变异体更靠近HAP表面。通过对5个HAP晶面N-末端和C-末端的21次SS核磁共振测量，对结构预测有偏差。LRAP的预测折叠在所有研究的HAP面上都是相似的，不考虑磷酸化。与实验观察基本一致，LRAP的预测结构在N-末端结构域有一个螺旋-转弯-螺旋基序，在C-末端结构域有一些螺旋，并且磷酸化变体的N-末端结构域与HAP的结合比非磷酸化变体的N-末端结构域更紧密。对这两个变体的预测都显示了{010}HAP晶面的一些潜在的结合特异性，进一步支持釉原蛋白阻止晶体在a和b面上的生长，以允许c轴上的拉长晶体。
The formation of biogenic materials requires the interaction of organic molecules with the mineral phase. In forming enamel, the amelogenin proteins contribute to the mineralization of hydroxyapatite (HAp). Leucine-rich amelogenin protein (LRAP) is a naturally occurring splice variant of amelogenin that comprises amelogenin's predicted HAp binding domains. We determined the partial structure of phosphorylated and non-phosphorylated LRAP variants bound to HAp using combined solid-state NMR (ssNMR) and ssNMR-biased computational structure prediction. New ssNMR measurements in the N-terminus indicate a largely extended structure for both variants, though some measurements are consistent with a partially helical N-terminal segment. The N-terminus of the phosphorylated variant is found to be consistently closer to the HAp surface than the non-phosphorylated variant. Structure prediction was biased using 21 ssNMR measurements in the N- and C-terminus at five HAp crystal faces. The predicted fold of LRAP is similar at all HAp faces studied, regardless of phosphorylation. Largely consistent with experimental observations, LRAP's predicted structure is relatively extended with a helix-turn-helix motif in the N-terminal domain and some helix in the C-terminal domain, and the N-terminal domain of the phosphorylated variant binds HAp more closely than the N-terminal domain of the non-phosphorylated variant. Predictions for both variants show some potential binding specificity for the {010} HAp crystal face, providing further support that amelogenins block crystal growth on the a and b faces to allow elongated crystals in the c-axis.
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影响因子：
2.7
作者：
Hu, Jan C. -C.;Chun, Yong-Hee P.;Simmer, James P.
通讯作者：
Simmer, James P.
影响因子：
4.4
作者：
BENNETT, AE;RIENSTRA, CM;GRIFFIN, RG
通讯作者：
GRIFFIN, RG
DOI：
10.1016/j.bbapap.2010.03.006
发表时间：
2010-09-01
影响因子：
3.2
作者：
Buchko, Garry W.;Tarasevich, Barbara J.;Shaw, Wendy J.
通讯作者：
Shaw, Wendy J.
影响因子：
0.9
作者：
Buchko, Garry W.;Bekhazi, Jacky;Shaw, Wendy J.
通讯作者：
Shaw, Wendy J.
影响因子：
4.2
作者：
AOBA, T;FUKAE, M;MORENO, EC
通讯作者：
MORENO, EC