1XOF

Heterooligomeric Beta Beta Alpha Miniprotein

1XOF の概要

• エントリーDOI: 10.2210/pdb1xof/pdb
• 関連するPDBエントリー: 1SN9 1SNA 1SNE
• 分子名称: BBAhetT1 (3 entities in total)
• 機能のキーワード: protein design, heterooligomer, heterotetramer, de novo protein
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 5187.89

構造登録者

Ali, M.H.,Taylor, C.M.,Grigoryan, G.,Allen, K.N.,Imperiali, B.,Keating, A.E. (登録日: 2004-10-06, 公開日: 2005-02-01, 最終更新日: 2026-03-18)

主引用文献

Ali, M.H.,Taylor, C.M.,Grigoryan, G.,Allen, K.N.,Imperiali, B.,Keating, A.E.
Design of a Heterospecific, Tetrameric, 21-Residue Miniprotein with Mixed alpha/beta Structure.
Structure, 13:225-234, 2005

PubMed Abstract: The study of short, autonomously folding peptides, or "miniproteins," is important for advancing our understanding of protein stability and folding specificity. Although many examples of synthetic alpha-helical structures are known, relatively few mixed alpha/beta structures have been successfully designed. Only one mixed-secondary structure oligomer, an alpha/beta homotetramer, has been reported thus far. In this report, we use structural analysis and computational design to convert this homotetramer into the smallest known alpha/beta-heterotetramer. Computational screening of many possible sequence/structure combinations led efficiently to the design of short, 21-residue peptides that fold cooperatively and autonomously into a specific complex in solution. A 1.95 A crystal structure reveals how steric complementarity and charge patterning encode heterospecificity. The first- and second-generation heterotetrameric miniproteins described here will be useful as simple models for the analysis of protein-protein interaction specificity and as structural platforms for the further elaboration of folding and function.

PubMed: 15698566
DOI: 10.1016/j.str.2004.12.009

実験手法

X-RAY DIFFRACTION (1.95 Å)