9KAP

Cryo-EM structure of glycopeptide fibril

9KAP の概要

• エントリーDOI: 10.2210/pdb9kap/pdb
• EMDBエントリー: 62213
• 分子名称: TYR-TYR-CYS-TYR-TYR, beta-D-glucopyranuronic acid (2 entities in total)
• 機能のキーワード: helical fibril, protein fibril
• 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: 11615.90

構造登録者

Xia, W.C.,Liu, C. (登録日: 2024-10-29, 公開日: 2025-06-11, 最終更新日: 2025-06-25)

主引用文献

Xia, W.,Xu, Z.,Dong, H.,Zhang, S.,He, C.,Li, D.,Sun, B.,Dai, B.,Dong, S.,Liu, C.
Design and Structural Elucidation of Glycopeptide Fibrils: Emulating Glycosaminoglycan Functions for Biomedical Applications.
J.Am.Chem.Soc., 147:20132-20143, 2025

PubMed Abstract: Glycosaminoglycans (GAGs) are essential polysaccharides crucial for various cellular functions, such as cell proliferation, migration, and differentiation. However, their complex structure and variability from natural sources pose challenges for functional studies and therapeutic applications. In this study, we engineered a glycopeptide that assembles into fibrils, emulating the functional attributes of GAGs. Utilizing cryo-EM, we elucidated the atomic structure of the designed glycopeptide fibril, which is composed of three identical protofilaments intertwined into a left-handed helix and held together by a variety of intermolecular interactions. Remarkably, the functional sugar units, glucuronic acids, are orderly positioned on the fibril surface, making them readily accessible to the solvent. This distinctive spatial configuration allows the designed glycopeptide fibril to effectively mimic key GAG functionalities, including the promotion of cell proliferation, cell migration, and osteogenic differentiation. Our findings offer a structural framework for designing glycan functionalities on glycopeptide fibrils and open avenues for developing glycopeptide-based materials with versatile biological activities. This work further enhances the potential of these materials for applications in therapeutic and regenerative medicine.

PubMed: 40448703
DOI: 10.1021/jacs.5c07039

実験手法

ELECTRON MICROSCOPY (3.2 Å)