2BAU

Solution NMR structure of the micelle-bound myristoylated N-terminal Arf6

2BAU の概要

• エントリーDOI: 10.2210/pdb2bau/pdb
• 分子名称: ADP-ribosylation factor 6, MYRISTIC ACID (2 entities in total)
• 機能のキーワード: micelle-bound, myristoylated peptide, signaling protein
• 細胞内の位置: Golgi apparatus: P62330
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1292.65

構造登録者

Gizachew, D. (登録日: 2005-10-14, 公開日: 2006-07-25, 最終更新日: 2024-11-20)

主引用文献

Gizachew, D.,Oswald, R.
NMR structural studies of the myristoylated N-terminus of ADP ribosylation factor 6 (Arf6).
Febs Lett., 580:4296-4301, 2006

PubMed Abstract: Arf proteins are guanine nucleotide binding proteins that are implicated in endocytotic pathways and vesicle trafficking. The two widely studied isoforms of Arf proteins (Arf1 and Arf6) have different cellular functions and localizations but similar structures. Arf proteins have an N-terminal helix with a covalently bound myristoyl group. Except structural models, there are no three dimensional structures of the myristoylated N-terminal peptide or the intact myristoylated Arf proteins. However, understanding the role of both the myristoyl group and the N-terminal helix based on the details of their molecular structures is of great interest. In the solution structure of myristoylated N-terminal peptide of Arf6 described here, the myristoyl group folds toward the N-terminus to interact with the hydrophobic residues in particular, the phenyl ring. Also, the structure of the dodecylphosphocholine (DPC) micelle-bound of the peptide together with paramagnetic studies showed that the myristoyl group is inserted into the micelle while residues V4-G10 interact with the surface of the micelle. The structural differences between the unbound and micelle-bound myristoylated N-terminal peptide of Arf6 involves the myristoyl group and the side chains of the hydrophobic residues.

PubMed: 16839550
DOI: 10.1016/j.febslet.2006.06.086

実験手法

SOLUTION NMR