Therapeutic sall4 peptide
一种中性、非极性的技术,应用在表达,4的,分离的肽接领域,能够解决缺乏靶标特异性等问题
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[0085] SALL4 binds to RBBp4 of NuRD
[0086] It was previously reported that SALL4WT binds to the NURD complex and blocks the SALL4-NuRD interaction. The histone-binding protein RBBp4 was hypothesized to be the SALL4-binding subunit in NuRD. To confirm the direct binding of SALL4 to RBBp4, a binding assay was performed using the 12 amino acid WT SALL4T (Figure 1). Using isothermal titration calorimetry, a direct interaction between SALL4 and the RBBp4 subunit of the NURD complex was demonstrated. The 12-aa SALL4 peptide binds to the K of RBBp4 D 1.04±0.06μM ( Figure 1A ). The binding kinetics were further confirmed using surface plasmon resonance, where the binding K between the SALL4 peptide and RBBp4 D Calculated to be 1.5 μM (k on =16830±460M -1 the s -1 ;k off=0.026±0.00045s -1 )( Figure 1B ). These results demonstrate that SALL4 directly binds to the NuRD complex through the NuRD subunit RBBp4.
[0087] Crystal structure of the RBBp4-SALL4 complex
[0088]...
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