1RH4

RH4 DESIGNED RIGHT-HANDED COILED COIL TETRAMER

1RH4 の概要

• エントリーDOI: 10.2210/pdb1rh4/pdb
• 分子名称: RIGHT-HANDED COILED COIL TETRAMER, ISOPROPYL ALCOHOL (3 entities in total)
• 機能のキーワード: de novo design, coiled coil
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3817.81

構造登録者

Harbury, P.B.,Plecs, J.J.,Tidor, B.,Alber, T.,Kim, P.S. (登録日: 1998-10-07, 公開日: 1998-12-02, 最終更新日: 2024-11-20)

主引用文献

Harbury, P.B.,Plecs, J.J.,Tidor, B.,Alber, T.,Kim, P.S.
High-resolution protein design with backbone freedom.
Science, 282:1462-1467, 1998

PubMed Abstract: Recent advances in computational techniques have allowed the design of precise side-chain packing in proteins with predetermined, naturally occurring backbone structures. Because these methods do not model protein main-chain flexibility, they lack the breadth to explore novel backbone conformations. Here the de novo design of a family of alpha-helical bundle proteins with a right-handed superhelical twist is described. In the design, the overall protein fold was specified by hydrophobic-polar residue patterning, whereas the bundle oligomerization state, detailed main-chain conformation, and interior side-chain rotamers were engineered by computational enumerations of packing in alternate backbone structures. Main-chain flexibility was incorporated through an algebraic parameterization of the backbone. The designed peptides form alpha-helical dimers, trimers, and tetramers in accord with the design goals. The crystal structure of the tetramer matches the designed structure in atomic detail.

PubMed: 9822371
DOI: 10.1126/science.282.5393.1462

実験手法

X-RAY DIFFRACTION (1.9 Å)