2bao
From Proteopedia
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Solution NMR structure of the myristoylated N-terminal fragment of Arf6
Overview
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.
About this Structure
2BAO is a Single protein structure of sequence from [1] with MYR as ligand. Full crystallographic information is available from OCA.
Reference
NMR structural studies of the myristoylated N-terminus of ADP ribosylation factor 6 (Arf6)., Gizachew D, Oswald R, FEBS Lett. 2006 Jul 24;580(17):4296-301. Epub 2006 Jul 7. PMID:16839550
Page seeded by OCA on Mon Nov 12 21:00:22 2007
Categories: Single protein | Gizachew, D. | MYR | Arf6 | Myristoyl | N-terminal
