Intramolecular interaction in the tail of Acanthamoeba myosin IC between the SH3 domain and a putative pleckstrin homology domain.
Intramolecular interaction in the tail of Acanthamoeba myosin IC between the SH3 domain and a putative pleckstrin homology domain.
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棘阿米巴肌球蛋白 IC 尾部 SH3 结构域和假定的 pleckstrin 同源结构域之间的分子内相互作用。
DOI：
10.1073/pnas.0610231104
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发表时间：
2007
影响因子：
11.1
通讯作者：
Gruschus,JamesM
中科院分区：
文献类型：
--
作者：
Hwang,Kae-Jung;Mahmoodian,Fatemeh;Ferretti,JamesA;Korn,EdwardD;Gruschus,JamesM
facanthamoebamyosin IC （AMIC）重链的466-aa尾部包括n端220个残基基区（BR）、56个残基Gly/Pro/ ala富区（GPA1）、55个残基Src同源3 （SH3）结构域和c端135个残基Gly/Pro/ ala富区（GPA2）。先前的冷冻电子显微镜显示，AMIC尾部折叠在自身上，这表明它的N端和c端区域之间可能存在相互作用。我们现在展示了细菌表达的全长尾的NMR谱与单独表达的BR和GPA1-SH3-GPA2 （GSG）区域的谱之和之间的具体差异。这些结果表明，在全长尾巴的两个子域之间的相互作用。根据核磁共振数据，我们可以确定BR和GSG中参与这些相互作用的许多残基。通过将同源性建模与核磁共振数据相结合，我们在BR中发现了一个假定的pleckstrin同源（PH）结构域，并表明PH结构域与SH3结构域相互作用。
The 466-aa tail of the heavy chain ofAcanthamoebamyosin IC (AMIC) comprises an N-terminal 220-residue basic region (BR) followed by a 56-residue Gly/Pro/Ala-rich region (GPA1), a 55-residue Src homology 3 (SH3) domain, and a C-terminal 135-residue Gly/Pro/Ala-rich region (GPA2). Cryo-electron microscopy of AMIC had shown previously that the AMIC tail is folded back on itself, suggesting the possibility of interactions between its N- and C-terminal regions. We now show specific differences between the NMR spectrum of bacterially expressed full-length tail and the sum of the spectra of individually expressed BR and GPA1-SH3-GPA2 (GSG) regions. These results are indicative of interactions between the two subdomains in the full-length tail. From the NMR data, we could assign many of the residues in BR and GSG that are involved in these interactions. By combining homology modeling with the NMR data, we identify a putative pleckstrin homology (PH) domain within BR, and show that the PH domain interacts with the SH3 domain.