Source:http://linkedlifedata.com/resource/pubmed/id/16156658
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
37
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pubmed:dateCreated |
2005-9-13
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pubmed:abstractText |
Many protein-protein and protein-nucleic acid interactions involve coupled folding and binding of at least one of the partners. Here, we propose a protein structural element or feature that mediates the binding events of initially disordered regions. This element consists of a short region that undergoes coupled binding and folding within a longer region of disorder. We call these features "molecular recognition elements" (MoREs). Examples of MoREs bound to their partners can be found in the alpha-helix, beta-strand, polyproline II helix, or irregular secondary structure conformations, and in various mixtures of the four structural forms. Here we describe an algorithm that identifies regions having propensities to become alpha-helix-forming molecular recognition elements (alpha-MoREs) based on a discriminant function that indicates such regions while giving a low false-positive error rate on a large collection of structured proteins. Application of this algorithm to databases of genomics and functionally annotated proteins indicates that alpha-MoREs are likely to play important roles protein-protein interactions involved in signaling events.
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pubmed:grant | |
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 |
Sep
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
44
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12454-70
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:16156658-Binding Sites,
pubmed-meshheading:16156658-Databases, Protein,
pubmed-meshheading:16156658-Kinetics,
pubmed-meshheading:16156658-Models, Molecular,
pubmed-meshheading:16156658-Models, Theoretical,
pubmed-meshheading:16156658-Protein Binding,
pubmed-meshheading:16156658-Protein Conformation,
pubmed-meshheading:16156658-Protein Folding,
pubmed-meshheading:16156658-Protein Structure, Secondary,
pubmed-meshheading:16156658-Proteins
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pubmed:year |
2005
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pubmed:articleTitle |
Coupled folding and binding with alpha-helix-forming molecular recognition elements.
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pubmed:affiliation |
Molecular Kinetics Inc., 6201 La Pas Trail, Suite 160, Indianapolis, Indiana 46268, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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