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首页> 外文期刊>Biochemistry >Identification of Tyrosine Residues Involved in Ligand Recognition by the Phosphatidylinositol 3-Kinase Src Homology 3 Domain: Circular Dichroism and UV Resonance Raman Studies
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Identification of Tyrosine Residues Involved in Ligand Recognition by the Phosphatidylinositol 3-Kinase Src Homology 3 Domain: Circular Dichroism and UV Resonance Raman Studies

机译：鉴定磷脂酰肌醇3-激酶Src同源性3域中涉及配体识别的酪氨酸残基：圆二色性和紫外共振拉曼研究

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Src homology 3 (SH3) domains are small noncatalytic protein modules capable of mediating protein0protein interactions. We previously demonstrated that the association of a ligand peptide RLP1 (RKLPPRPSK) causes environmental and structural changes of Trp55 and some of seven Tyr resiiduues in the phosphatidylinositol 3-kinase (P13K) SH3 domain by circular dichroism (CD) and 235-nm excited UV resonance Raman (UVRR) spectroscopies [Okishio, N., et al. (2000) Biopolymers 57, 208-217]. In this work, the affected Tyr residues were identified as Tyr12, Tyr14, and Tyr73 by the CD analysis of a series of mutants, in which every single Tyr residue was replced by a Phe residue. Among these three residuues, Tyr14 was found to be a main contributor to the UVRR spectral change upon the RLP1 binding. Interestingly, CD and UVRR analyses revealed that RLP1 associates with the Y14F and Y14H mutants in diffferent ways. These results suggest that Tyr14 plays a crucial role in the ligand recognition, and the amino acid substitution at Tyr14 affects the mode of PI3K SH3-ligand interaction. Our findings give an insight into how SH3 domains can produce diversity and specificity to transduce signaling within cells.
机译：Src同源性3（SH3）域是能够介导蛋白质相互作用的小型非催化蛋白质模块。我们以前证明配体肽RLP1（RKLPPRPSK）的结合会通过圆二色性（CD）和235 nm激发的UV引起磷脂酰肌醇3-激酶（P13K）SH3域中Trp55和七个Tyr残基中的一些发生环境和结构变化共振拉曼光谱（UVRR）[Okishio，N.，et al。 （2000）生物聚合物57，208-217]。在这项工作中，通过一系列突变体的CD分析，将受影响的Tyr残基鉴定为Tyr12，Tyr14和Tyr73，其中每个单个Tyr残基都被Phe残基所取代。在这三个残基中，发现Tyr14是RLP1结合后UVRR光谱变化的主要贡献者。有趣的是，CD和UVRR分析表明RLP1以不同的方式与Y14F和Y14H突变体缔合。这些结果表明，Tyr14在配体识别中起着至关重要的作用，并且Tyr14处的氨基酸取代会影响PI3K SH3-配体相互作用的方式。我们的发现提供了关于SH3结构域如何产生多样性和特异性以转导细胞内信号传导的见解。

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