此論文旨在探討兩蛋白質：人類細胞中的肝癌衍生生長因子(hHDGF)與乙烯受體之訊號調節區域(ETR1-RD)其結構與動力學的特性。
在人類細胞中的肝癌衍生生長因子(hHDGF)中，HATH domains 是HDGF相關蛋白質家族(HDGF-related proteins, HRPs)中，一段具有高度保留性的區域，而這段區域皆包含特殊的PWWP motif 且會與肝素/硫酸乙醯肝素(heparin/heparan sulfate)，DNA和甲基化的組織蛋白胜肽片段(methylated histone peptide)作鍵結來調控細胞功能。根據PWWP motif 中的第一個殘基不同可區分為兩種類型：P-類型為PHWP (Pro-His-Trp-Pro)，其中P-類型為PHWP (Pro-His-Trp-Pro)，HATH較穩定且皆已解出結構；A-類型為AHWP(Ala-His-Trp-Pro) ，但HATH在水溶液中較不穩定，因此我們探討兩者之間包含結構，動力學及配基結合能力的不同。根據NMR 15N 弛豫實驗分析，觀察到蛋白質骨架動態主要發生在N端的 β-barrel 及C端helix bundle之介面。在AHWP所在之 β1/β2 loop具有高度結構彈性去幫助HATH-HATH結合。在與肝素及長鏈DNA結合中，A-類型HATH展現出較高層次聚合的傾向。
在第二個蛋白質例子中，乙烯受體(ETR1)與乙烯氣體調控多種植物生理活動。雖然其下游調控者與其分子辨識機制還未確定，目前推測乙烯受體在細胞質內的訊息，是與訊號調節區域(receiver domain，RD)有關的雙元件系統方式(two-component system，TCS)作傳遞。此論文利用NMR方法去探討乙烯受體的訊號調節區域(ETR1-RD)其結構與動力學特性。結合NMR技術所得之骨架化學位移與結構計算得知ETR1-RD在水溶液下的結構與X-ray結構是相似的，但ETR1-RD在水溶液下是單體結構而X-ray結構則是雙體。特別的是，在NMR技術中沒有觀察到ETR1-RD的磷酸化形成。與其他訊號調節區域蛋白質的動態結構相比，我們猜測蛋白質骨架的彈性會去影響磷酸化形成。而ETR1-RD在此被歸類為非典型的訊號調節區域。

We investigated the structural and dynamic characters of two proteins in the study: Hepatoma-derived growth factor (HDGF) and receiver domain of ethylene receptor 1 (ETR1-RD).
In the first case, HDGF-related proteins (HRPs) contain conserved N-terminal HATH domains with a characteristic PWWP motif. The HATH domains have drawn attention because of the binding with heparin/heparan sulfate, DNA and methylated histone peptide. Depending on the sequence of the PWWP motif, HATHs are classified into P-type (Pro-His-Trp-Pro) and A-type (Ala-His-Trp-Pro). A-type HATH is highly unstable in solution and P-type HATH has available structure. We evaluated the difference on structure, dynamics and ligand binding. Analysis of NMR backbone 15N relaxations revealed additional backbone dynamics in the interface between the b-barrel and the C-terminal helix bundle. The β1/β2 loop, where the AHWP sequence is located, has great structural flexibility, which aids HATH-HATH interaction. A-type HATH, therefore, shows a tendency toward higher-order aggregation when binding with heparin and DNA oligomers.
In the second case, ETR1, in response to ethylene, plays versatile roles in plant physiology. Although the downstream regulators have been identified, the molecular recognition remains unknown. It has been speculated that the cytoplasmic signaling of ETR1 adopts a two-component system involving the conserved receiver domain (RD). We used NMR method to investigate the structure and dynamics of ETR1-RD. Combining NMR backbone chemical shifts into the structural calculation, we defined the solution ETR1-RD structure similar to X-ray structure, but ETR1-RD is a monomer, not the dimer observed in X-ray crystal. Notably, NMR investigation reported no phosphorylation for ETR1-RD. Comparing the backbone dynamics to other receiver regulators, we suspect the backbone flexibility is critical to determine the phosphorylation property. ETR1-RD is an atypical receiver regulator.

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