1HQJ

CRYSTAL STRUCTURE OF A DE NOVO DESIGNED TRIMERIC COILED-COIL PEPTIDE

1HQJ の概要

• エントリーDOI: 10.2210/pdb1hqj/pdb
• 関連するPDBエントリー: 1D7M 1GCM
• 分子名称: ZJU-GLU-LEU-GLU-ALA-ARG-ILE-ARG-GLU-LEU-GLU-ALA-ARG-ILE-LYS-NH2, LEAD (II) ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: coiled coil, de novo design, alpha-helix, trimer, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 26624.58

構造登録者

Burkhard, P.,Meier, M.,Lustig, A. (登録日: 2000-12-18, 公開日: 2001-03-14, 最終更新日: 2024-04-24)

主引用文献

Burkhard, P.,Meier, M.,Lustig, A.
Design of a minimal protein oligomerization domain by a structural approach.
Protein Sci., 9:2294-2301, 2000

PubMed Abstract: Because of the simplicity and regularity of the alpha-helical coiled coil relative to other structural motifs, it can be conveniently used to clarify the molecular interactions responsible for protein folding and stability. Here we describe the de novo design and characterization of a two heptad-repeat peptide stabilized by a complex network of inter- and intrahelical salt bridges. Circular dichroism spectroscopy and analytical ultracentrifugation show that this peptide is highly alpha-helical and 100% dimeric tinder physiological buffer conditions. Interestingly, the peptide was shown to switch its oligomerization state from a dimer to a trimer upon increasing ionic strength. The correctness of the rational design principles used here is supported by details of the atomic structure of the peptide deduced from X-ray crystallography. The structure of the peptide shows that it is not a molten globule but assumes a unique, native-like conformation. This de novo peptide thus represents an attractive model system for the design of a molecular recognition system.

PubMed: 11206050

実験手法

X-RAY DIFFRACTION (1.2 Å)