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首页> 外文期刊>Biochemistry >Redesign of a WW Domain Peptide for Selective Recognition of Single-Stranded DNA
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Redesign of a WW Domain Peptide for Selective Recognition of Single-Stranded DNA

机译：重新设计用于选择性识别单链DNA的WW域肽

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A beta-sheet miniprotein based on the FBP11 WW1 domain sequence has been redesigned for the molecular recognition of ssDNA A previous report showed that a beta-hairpin peptide dimer, (WKWK)(2), binds ssDNA with low micromolar affinity but with little selectivity over duplex DNA. This report extends those studies to a three-stranded beta-sheet miniprotein designed to mimic the OB-fold. The new peptide binds ssDNA with low micromolar affinity and shows about 10-fold selectivity for ssDNA over duplex DNA. The redesigned peptide no longer binds its native ligand, the polyproline helix, confirming that the peptide has been redesigned for the function of binding ssDNA. Structural studies provide evidence that this peptide consists of a well-structured beta-hairpin made of strands 2 and 3 with a less structured first strand that provides affinity for ssDNA but does not improve the stability of the full peptide. These studies provide insight into protein DNA interactions as well as a novel example of protein redesign.
机译：基于FBP11 WW1结构域序列的β-折叠小蛋白已经过重新设计，可用于ssDNA的分子识别。先前的报道显示，β-发夹肽二聚体（WKWK）（2）以低微摩尔亲和力但选择性很小的方式结合ssDNA。双链DNA。该报告将这些研究扩展到旨在模拟OB折叠的三链β-折叠小蛋白。这种新肽以低微摩尔亲和力与ssDNA结合，相对于双链DNA显示出约10倍的ssDNA选择性。重新设计的肽不再结合其天然配体多脯氨酸螺旋，从而证实该肽已针对结合ssDNA的功能进行了重新设计。结构研究提供了证据，表明该肽由结构良好的β-发夹组成，该结构由链2和3组成，第一链结构较少，可提供对ssDNA的亲和力，但不会提高完整肽的稳定性。这些研究提供了对蛋白质DNA相互作用的深入了解，以及蛋白质重新设计的新实例。

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