3IPN

Crystal Structure of fluorine and methyl modified collagen: (mepFlpgly)7

3IPN の概要

• エントリーDOI: 10.2210/pdb3ipn/pdb
• 分子名称: Non-natural Collagen, CARBONATE ION (3 entities in total)
• 機能のキーワード: collagen, fluorinated methylated collagen, nonnatural amino acid, structural protein
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 12246.70

構造登録者

Satyshur, K.A.,Shoulders, M.D.,Raines, R.T.,Forest, K.T. (登録日: 2009-08-18, 公開日: 2010-02-02, 最終更新日: 2024-11-06)

主引用文献

Shoulders, M.D.,Satyshur, K.A.,Forest, K.T.,Raines, R.T.
Stereoelectronic and steric effects in side chains preorganize a protein main chain.
Proc.Natl.Acad.Sci.USA, 107:559-564, 2010

PubMed Abstract: Preorganization is shown to endow a protein with extraordinary conformational stability. This preorganization is achieved by installing side-chain substituents that impose stereoelectronic and steric effects that restrict main-chain torsion angles. Replacing proline residues in (ProProGly)(7) collagen strands with 4-fluoroproline and 4-methylproline leads to the most stable known triple helices, having T ( m ) values that are increased by > 50 degrees C. Differential scanning calorimetry data indicate an entropic basis to the hyperstability, as expected from an origin in preorganization. Structural data at a resolution of 1.21 A reveal a prototypical triple helix with insignificant deviations to its main chain, even though 2/3 of the residues are nonnatural. Thus, preorganization of a main chain by subtle changes to side chains can confer extraordinary conformational stability upon a protein without perturbing its structure.

PubMed: 20080719
DOI: 10.1073/pnas.0909592107

実験手法

X-RAY DIFFRACTION (1.21 Å)