1v6r

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[[Image:1v6r.jpg|left|200px]]
 
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==Solution Structure of Endothelin-1 with its C-terminal Folding==
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The line below this paragraph, containing "STRUCTURE_1v6r", creates the "Structure Box" on the page.
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<StructureSection load='1v6r' size='340' side='right'caption='[[1v6r]]' 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'>[[1v6r]] 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=1V6R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V6R FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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, 20 models</td></tr>
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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=1v6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v6r OCA], [https://pdbe.org/1v6r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v6r RCSB], [https://www.ebi.ac.uk/pdbsum/1v6r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v6r ProSAT]</span></td></tr>
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{{STRUCTURE_1v6r| PDB=1v6r | SCENE= }}
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</table>
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== Function ==
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'''Solution Structure of Endothelin-1 with its C-terminal Folding'''
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[https://www.uniprot.org/uniprot/EDN1_HUMAN EDN1_HUMAN] Endothelins are endothelium-derived vasoconstrictor peptides.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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==Overview==
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Distributed computing has been implemented to the solution structure determination of endothelin-1 to evaluate efficiency of the method for NMR constraint-based structure calculations. A key target of the investigation was determination of the C-terminal folding of the peptide, which had been dispersed in previous studies of NMR, despite its pharmacological significances. With use of tens of thousands of random initial structures to explore the conformational space comprehensively, we determined high-resolution structures with good convergences of C-terminal as well as previously defined N-terminal structures. The previous studies had missed the C-terminal convergence because of initial structure dependencies trapped in localized folding of the N-terminal region, which are strongly constricted by two disulfide bonds.
Distributed computing has been implemented to the solution structure determination of endothelin-1 to evaluate efficiency of the method for NMR constraint-based structure calculations. A key target of the investigation was determination of the C-terminal folding of the peptide, which had been dispersed in previous studies of NMR, despite its pharmacological significances. With use of tens of thousands of random initial structures to explore the conformational space comprehensively, we determined high-resolution structures with good convergences of C-terminal as well as previously defined N-terminal structures. The previous studies had missed the C-terminal convergence because of initial structure dependencies trapped in localized folding of the N-terminal region, which are strongly constricted by two disulfide bonds.
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==About this Structure==
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Distributed computing and NMR constraint-based high-resolution structure determination: applied for bioactive Peptide endothelin-1 to determine C-terminal folding.,Takashima H, Mimura N, Ohkubo T, Yoshida T, Tamaoki H, Kobayashi Y J Am Chem Soc. 2004 Apr 14;126(14):4504-5. PMID:15070353<ref>PMID:15070353</ref>
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1V6R is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V6R OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Distributed computing and NMR constraint-based high-resolution structure determination: applied for bioactive Peptide endothelin-1 to determine C-terminal folding., Takashima H, Mimura N, Ohkubo T, Yoshida T, Tamaoki H, Kobayashi Y, J Am Chem Soc. 2004 Apr 14;126(14):4504-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15070353 15070353]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 1v6r" style="background-color:#fffaf0;"></div>
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[[Category: Kobayashi, Y.]]
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== References ==
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[[Category: Mimura, N.]]
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<references/>
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[[Category: Ohkubo, T.]]
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__TOC__
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[[Category: Takashima, H.]]
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</StructureSection>
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[[Category: Tamaoki, H.]]
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[[Category: Homo sapiens]]
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[[Category: Yoshida, T.]]
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[[Category: Large Structures]]
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[[Category: A-helix]]
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[[Category: Kobayashi Y]]
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[[Category: C-terminal folding]]
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[[Category: Mimura N]]
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[[Category: Cardiovascular bioactive peptide]]
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[[Category: Ohkubo T]]
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[[Category: Endothelin]]
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[[Category: Takashima H]]
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[[Category: G-protein coupled-receptor ligand]]
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[[Category: Tamaoki H]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:09:28 2008''
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[[Category: Yoshida T]]

Current revision

Solution Structure of Endothelin-1 with its C-terminal Folding

PDB ID 1v6r

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