4M6A

N-Terminal beta-Strand Swapping in a Consensus Derived Alternative Scaffold Driven by Stabilizing Hydrophobic Interactions

4M6A の概要

• エントリーDOI: 10.2210/pdb4m6a/pdb
• 関連するPDBエントリー: 3tes
• 分子名称: Tencon (2 entities in total)
• 機能のキーワード: tencon, fn3-like domain, alternative scaffold, b-strand swapping, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 99019.54

構造登録者

Luo, J.,Teplyakov, A.,Obmolova, G.,Malia, T.J.,Chan, W.,Jocobs, S.A.,O'neil, K.T.,Gilliland, G.L. (登録日: 2013-08-09, 公開日: 2014-02-26, 最終更新日: 2023-09-20)

主引用文献

Luo, J.,Teplyakov, A.,Obmolova, G.,Malia, T.J.,Chan, W.,Jacobs, S.A.,O'Neil, K.T.,Gilliland, G.L.
N-terminal beta-strand swapping in a consensus-derived alternative scaffold driven by stabilizing hydrophobic interactions.
Proteins, 82:1527-1533, 2014

PubMed Abstract: The crystal structure of an N-terminal β-strand-swapped consensus-derived tenascin FN3 alternative scaffold has been determined. A comparison with the unswapped structure reveals that the side chain of residue F88 orients differently and packs more tightly with the hydrophobic core of the domain. Dimer formation also results in the burial of a hydrophobic patch on the surface of the domain. Thus, it appears that tighter packing of F88 in the hydrophobic core and burial of surface hydrophobicity provide the driving forces for the N-terminal β-strand swapping, leading to the formation of a stable compact dimer.

PubMed: 24464739
DOI: 10.1002/prot.24517

実験手法

X-RAY DIFFRACTION (2.71 Å)