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首页> 外文期刊>Biochemistry >A Focal Adhesion Kinase-Derived Peptide Binds the Src SH3 Domain in Two Orientations, As Demonstrated Using Paramagnetic Nuclear Magnetic Resonance
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A Focal Adhesion Kinase-Derived Peptide Binds the Src SH3 Domain in Two Orientations, As Demonstrated Using Paramagnetic Nuclear Magnetic Resonance

机译：局灶性粘附激酶衍生的肽绑定Src SH3域在两个方向上，如使用顺磁核磁共振所示。

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摘要

SH3 binding peptides contain polyproline helices and are classified according to their binding orientations as N-to-C-terminal or C-to-N-terminal. We have tested the hypothesis that such a peptide binds in both orientations but with different populations. A focal adhesion kinase (FAK)-derived peptide was tested for its binding orientation on the Src SH3 domain. Paramagnetic tags were introduced at several positions on the SH3 domain, and on the basis of the paramagnetic relaxation enhancements (PREs) of the amide protons, the positions of the paramagnetic centers were determined. Two peptides were synthesized with C-13-enriched Ala or Pro, at the N-terminal or C-terminal side of the peptide, and the intermolecular PREs were measured. The results provide compelling evidence that the FAK-derived peptide binds the SH3 domain in two orientations. In the major state, the SH3 domain binds the peptide in the N-C orientation, whereas 20% of the time, the peptide binds in the C-N orientation. We conclude that the distinction between N-C and C-N orientations, which is based on crystal structures, might be artificial. The pseudosymmetric nature of the polyproline helix might allow for binding in both orientations in the solution state.
机译：SH3结合肽含有多脯氨酸螺旋，并根据其结合方向分为N-C端或C-N端。我们已经检验了这样的假设，即这种肽在两个方向上都结合但具有不同的种群。测试了粘着斑激酶（FAK）衍生的肽在Src SH3域上的结合方向。将顺磁标签引入到SH3域的几个位置，并基于酰胺质子的顺磁弛豫增强（PRE），确定了顺磁中心的位置。用富含C-13的Ala或Pro在肽的N-末端或C-末端侧合成了两个肽，并测量了分子间的PRES。该结果提供了令人信服的证据，即FAK衍生的肽在两个方向上结合SH3结构域。在主要状态下，SH3结构域以N-C方向结合肽，而20％的时间，肽以C-N方向结合。我们得出结论，基于晶体结构的N-C和C-N取向之间的区别可能是人为的。聚脯氨酸螺旋的假对称性质可能允许溶液状态在两个方向上结合。

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