Source:http://linkedlifedata.com/resource/pubmed/id/10403428
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1999-10-12
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pubmed:abstractText |
Two-dimensional nuclear magnetic resonance techniques and a combination of distance geometry and molecular dynamics calculations were utilised to determine the three dimensional solution structure of an ET-1 analogue, ET-1[Aib1,3,11,15, Nle7], in a methanol-d3/water co-solvent. The modelled structure shows that the peptide folds into a consistent alpha-helical conformation between residues Ser4-His16 while the C-terminus prefers no fixed conformation. Our studies confirm that the disulphide links which are normally associated with the endothelin family of neuropeptides are not important for the formation of a helical conformation in solution. This full length, modified, synthetic linear ET-1 analogue plays a vital role towards designing endothelin receptor agonists. Structure activity relationships are discussed in terms of the conformational features of the calculated structure.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Disulfides,
http://linkedlifedata.com/resource/pubmed/chemical/Endothelin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Histidine,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/Solutions
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0197-0186
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
35
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
35-45
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pubmed:dateRevised |
2009-9-29
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pubmed:meshHeading |
pubmed-meshheading:10403428-Amino Acid Sequence,
pubmed-meshheading:10403428-Computer Graphics,
pubmed-meshheading:10403428-Disulfides,
pubmed-meshheading:10403428-Endothelin-1,
pubmed-meshheading:10403428-Histidine,
pubmed-meshheading:10403428-Models, Molecular,
pubmed-meshheading:10403428-Molecular Sequence Data,
pubmed-meshheading:10403428-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:10403428-Protein Structure, Secondary,
pubmed-meshheading:10403428-Serine,
pubmed-meshheading:10403428-Software,
pubmed-meshheading:10403428-Solutions
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pubmed:year |
1999
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pubmed:articleTitle |
A linear endothelin-1 analogue: solution structure of ET-1[Aib1,3,11,15, Nle7] by nuclear magnetic resonance spectroscopy and molecular modelling.
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pubmed:affiliation |
Department of Chemistry, University of Edinburgh, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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