Jonckheere V, Lambrechts A, Vandekerckhove J, Ampe C
Flanders Interuniversity Institute of Biotechnology, Department of Biochemistry, Faculty of Medicine, Universiteit Gent, Ghent, Belgium.
FEBS Lett. 1999 Mar 26;447(2-3):257-63. doi: 10.1016/s0014-5793(99)00293-8.
Profilin II dimers bind the (GP5)3 peptide derived from VASP with an affinity of approximately 0.5 microM. The resulting profilin II-peptide complex overcomes the combined capacity of thymosin beta4 and profilin II to inhibit actin nucleation and restores the extent of filament formation. We do not observe such an effect when barbed filament ends are capped. Neither can profilin I, in the presence of the peptide, promote actin polymerization during its early phase consistent with a lower affinity. Since a Pro17 peptide-profilin II complex only partially restores actin polymerization, the glycine residues in the VASP peptide appear important.
丝切蛋白II二聚体以约0.5微摩尔的亲和力结合源自血管舒张刺激蛋白（VASP）的(GP5)3肽。由此产生的丝切蛋白II - 肽复合物克服了胸腺素β4和丝切蛋白II抑制肌动蛋白成核的联合能力，并恢复了丝状体形成的程度。当带刺丝状体末端被封闭时，我们没有观察到这种效应。在存在该肽的情况下，丝切蛋白I在其早期阶段也不能促进肌动蛋白聚合，这与较低的亲和力一致。由于Pro17肽 - 丝切蛋白II复合物仅部分恢复肌动蛋白聚合，VASP肽中的甘氨酸残基似乎很重要。
