3B83

Computer-Based Redesign of a beta Sandwich Protein Suggests that Extensive Negative Design Is Not Required for De Novo beta Sheet Design.

3B83 の概要

• エントリーDOI: 10.2210/pdb3b83/pdb
• 分子名称: TEN-D3 (2 entities in total)
• 機能のキーワード: beta sheet, computational redesigned protein, cell adhesion, egf-like domain, extracellular matrix, glycoprotein, phosphorylation, secreted, unknown function
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 89131.86

構造登録者

Hu, X.,Ke, H.,Kuhlman, B. (登録日: 2007-10-31, 公開日: 2008-11-04, 最終更新日: 2023-08-30)

主引用文献

Hu, X.,Wang, H.,Ke, H.,Kuhlman, B.
Computer-Based Redesign of a beta Sandwich Protein Suggests that Extensive Negative Design Is Not Required for De Novo beta Sheet Design.
Structure, 16:1799-1805, 2008

PubMed Abstract: The de novo design of globular beta sheet proteins remains largely an unsolved problem. It is unclear whether most designs are failing because the designed sequences do not have favorable energies in the target conformations or whether more emphasis should be placed on negative design, that is, explicitly identifying sequences that have poor energies when adopting undesired conformations. We tested whether we could redesign the sequence of a naturally occurring beta sheet protein, tenascin, with a design algorithm that does not include explicit negative design. Denaturation experiments indicate that the designs are significantly more stable than the wild-type protein and the crystal structure of one design closely matches the design model. These results suggest that extensive negative design is not required to create well-folded beta sandwich proteins. However, it is important to note that negative design elements may be encoded in the conformation of the protein backbone which was preserved from the wild-type protein.

PubMed: 19081056
DOI: 10.1016/j.str.2008.09.013

実験手法

X-RAY DIFFRACTION (2.4 Å)