The interwinding nature of protein protein interfaces and its implication for protein complex formation

Kei Yura*, Steven Hayward

*この研究の対応する著者

研究成果: Article査読

15 被引用数 (Scopus)

抄録

Motivation: Structural features at protein-protein interfaces can be studied to understand protein-protein interactions. It was noticed that in a dataset of 45 multimeric proteins the interface could either be described as flat against flat or protruding/interwound. In the latter, residues within one chain were surrounded by those in other chains, whereas in the former they were not. Results: A simple method was developed that could distinguish between these two types with results that matched those made by a human annotator. Applying this automatic method to a large dataset of 888 structures, chains at interfaces were categorized as non-surrounded or surrounded. It was found that the surrounded set had a significantly lower folding tendency using a sequence based measure, than the non-surrounded set. This suggests that before complexation, surrounded chains are relatively unstable and may be involved in 'fly-casting'. This is supported by the finding that terminal regions are overrepresented in the surrounded set.

本文言語English
論文番号btp563
ページ(範囲)3108-3113
ページ数6
ジャーナルBioinformatics
25
23
DOI
出版ステータスPublished - 2009 9月 29
外部発表はい

ASJC Scopus subject areas

  • 統計学および確率
  • 生化学
  • 分子生物学
  • コンピュータ サイエンスの応用
  • 計算理論と計算数学
  • 計算数学

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