2M9E

NMR solution structure of Pin1 WW domain mutant 5-1

2M9E の概要

• エントリーDOI: 10.2210/pdb2m9e/pdb
• 関連するPDBエントリー: 2M9F 2M9I 2M9J
• NMR情報: BMRB: 19291
• 分子名称: Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (1 entity in total)
• 機能のキーワード: n-glycosylation, enhanced aromatic sequon, ww domain, ch-pi interaction, isomerase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: Q13526
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3849.31

構造登録者

Enck, S.,Chen, W.,Price, J.L.,Powers, E.T.,Wong, C.,Dyson, H.J.,Kelly, J.W. (登録日: 2013-06-07, 公開日: 2013-06-26, 最終更新日: 2024-05-15)

主引用文献

Chen, W.,Enck, S.,Price, J.L.,Powers, D.L.,Powers, E.T.,Wong, C.H.,Dyson, H.J.,Kelly, J.W.
Structural and energetic basis of carbohydrate-aromatic packing interactions in proteins.
J.Am.Chem.Soc., 135:9877-9884, 2013

PubMed Abstract: Carbohydrate-aromatic interactions mediate many biological processes. However, the structure-energy relationships underpinning direct carbohydrate-aromatic packing interactions in aqueous solution have been difficult to assess experimentally and remain elusive. Here, we determine the structures and folding energetics of chemically synthesized glycoproteins to quantify the contributions of the hydrophobic effect and CH-π interactions to carbohydrate-aromatic packing interactions in proteins. We find that the hydrophobic effect contributes significantly to protein-carbohydrate interactions. Interactions between carbohydrates and aromatic amino acid side chains, however, are supplemented by CH-π interactions. The strengths of experimentally determined carbohydrate CH-π interactions do not correlate with the electrostatic properties of the involved aromatic residues, suggesting that the electrostatic component of CH-π interactions in aqueous solution is small. Thus, tight binding of carbohydrates and aromatic residues is driven by the hydrophobic effect and CH-π interactions featuring a dominating dispersive component.

PubMed: 23742246
DOI: 10.1021/ja4040472

実験手法

SOLUTION NMR