2bau

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[[Image:2bau.png|left|200px]]
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==Solution NMR structure of the micelle-bound myristoylated N-terminal Arf6==
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<StructureSection load='2bau' size='340' side='right' caption='[[2bau]], [[NMR_Ensembles_of_Models | 12 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2bau]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BAU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BAU FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bau OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bau RCSB], [http://www.ebi.ac.uk/pdbsum/2bau PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_2bau| PDB=2bau | SCENE= }}
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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<ref>PMID:16839550</ref>
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===Solution NMR structure of the micelle-bound myristoylated N-terminal Arf6===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_16839550}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2bau]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BAU OCA].
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</StructureSection>
[[Category: Gizachew, D.]]
[[Category: Gizachew, D.]]
[[Category: Micelle-bound]]
[[Category: Micelle-bound]]
[[Category: Myristoylated peptide]]
[[Category: Myristoylated peptide]]
[[Category: Signaling protein]]
[[Category: Signaling protein]]

Revision as of 08:27, 8 October 2014

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

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