Source:http://linkedlifedata.com/resource/pubmed/id/15474515
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2004-10-11
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pubmed:abstractText |
A number of subtypes of the alpha-adrenoceptor have been identified; however, knowledge of the three-dimensional structures of such membrane proteins is limited, and no crystal structure of an alpha-adrenoceptor is available to date. We have developed and analysed homology models of the alpha1A-adrenoceptor subtype based on the bovine rhodopsin crystal structure (1l9 h). Subsequent structural refinement was performed through molecular dynamics simulations using the Amber 7 suite of programs with a biphasic H2O/CHCl3/H2O cell utilised to mimic the receptor's natural membrane environment.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
12
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pubmed:volume |
324
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
916-21
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:15474515-Animals,
pubmed-meshheading:15474515-Cattle,
pubmed-meshheading:15474515-Computational Biology,
pubmed-meshheading:15474515-Crystallography, X-Ray,
pubmed-meshheading:15474515-Humans,
pubmed-meshheading:15474515-Models, Molecular,
pubmed-meshheading:15474515-Molecular Conformation,
pubmed-meshheading:15474515-Protein Conformation,
pubmed-meshheading:15474515-Protein Folding,
pubmed-meshheading:15474515-Receptors, Adrenergic, alpha-1,
pubmed-meshheading:15474515-Rhodopsin,
pubmed-meshheading:15474515-Software
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pubmed:year |
2004
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pubmed:articleTitle |
Computational development of an alpha1A-adrenoceptor model in a membrane mimic.
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pubmed:affiliation |
Department of Chemistry, Trinity College Dublin, Dublin 2, Ireland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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