2bao

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{{Seed}}
 
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[[Image:2bao.png|left|200px]]
 
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==Solution NMR structure of the myristoylated N-terminal fragment of Arf6==
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The line below this paragraph, containing "STRUCTURE_2bao", creates the "Structure Box" on the page.
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<StructureSection load='2bao' size='340' side='right'caption='[[2bao]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2bao]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BAO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BAO FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 12 models</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></td></tr>
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{{STRUCTURE_2bao| PDB=2bao | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bao OCA], [https://pdbe.org/2bao PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bao RCSB], [https://www.ebi.ac.uk/pdbsum/2bao PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bao ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ARF6_HUMAN ARF6_HUMAN] GTP-binding protein involved in protein trafficking; regulates endocytic recycling and cytoskeleton remodeling. May modulate vesicle budding and uncoating within the Golgi apparatus. Functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in the regulation of dendritic spine development (By similarity). Contributes to the regulation of dendritic branching and filopodia extension.<ref>PMID:7589240</ref> <ref>PMID:14978216</ref> <ref>PMID:11266366</ref>
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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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===Solution NMR structure of the myristoylated N-terminal fragment of Arf6===
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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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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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The line below this paragraph, {{ABSTRACT_PUBMED_16839550}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2bao" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16839550 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16839550}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Homo sapiens]]
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2BAO is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BAO OCA].
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[[Category: Large Structures]]
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[[Category: Gizachew D]]
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16839550 16839550]
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[[Category: Single protein]]
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[[Category: Gizachew, D.]]
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[[Category: Arf6]]
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[[Category: Myristoyl]]
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[[Category: N-terminal]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:40:59 2008''
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Current revision

Solution NMR structure of the myristoylated N-terminal fragment of Arf6

PDB ID 2bao

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