3T4F

Crystal Structure of a KGE Collagen Mimetic Peptide at 1.68 A

3T4F の概要

• エントリーDOI: 10.2210/pdb3t4f/pdb
• 関連するPDBエントリー: 3u29 6vzx
• 分子名称: collagen mimetic peptide (2 entities in total)
• 機能のキーワード: collagen mimetic peptide, triple helix, biosynthetic protein
• 由来する生物種: synthetic construct (artificial sequence)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 13370.25

構造登録者

Fallas, J.A.,Dong, J.,Miller, M.D.,Tao, Y.J.,Hartgerink, J.D. (登録日: 2011-07-25, 公開日: 2011-12-28, 最終更新日: 2023-09-13)

主引用文献

Fallas, J.A.,Dong, J.,Tao, Y.J.,Hartgerink, J.D.
Structural insights into charge pair interactions in triple helical collagen-like proteins.
J.Biol.Chem., 287:8039-8047, 2012

PubMed Abstract: The collagen triple helix is the most abundant protein fold in humans. Despite its deceptively simple structure, very little is understood about its folding and fibrillization energy landscape. In this work, using a combination of x-ray crystallography and nuclear magnetic resonance spectroscopy, we carry out a detailed study of stabilizing pair-wise interactions between the positively charged lysine and the negatively charged amino acids aspartate and glutamate. We find important differences in the side chain conformation of amino acids in the crystalline and solution state. Structures from x-ray crystallography may have similarities to the densely packed triple helices of collagen fibers whereas solution NMR structures reveal the simpler interactions of isolated triple helices. In solution, two distinct types of contacts are observed: axial and lateral. Such register-specific interactions are crucial for the understanding of the registration process of collagens and the overall stability of proteins in this family. However, in the crystalline state, there is a significant rearrangement of the side chain conformation allowing for packing interactions between adjacent helices, which suggests that charged amino acids may play a dual role in collagen stabilization and folding, first at the level of triple helical assembly and second during fibril formation.

PubMed: 22179819
DOI: 10.1074/jbc.M111.296574

実験手法

X-RAY DIFFRACTION (1.68 Å)