Source:http://linkedlifedata.com/resource/pubmed/id/20927343
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
9
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| pubmed:dateCreated |
2010-10-7
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| pubmed:abstractText |
Formin proteins utilize a conserved formin homology 2 (FH2) domain to nucleate new actin filaments. In mammalian diaphanous-related formins (DRFs) the FH2 domain is inhibited through an unknown mechanism by intramolecular binding of the diaphanous autoinhibitory domain (DAD) and the diaphanous inhibitory domain (DID).
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| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
1932-6203
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| pubmed:author | |
| pubmed:issnType |
Electronic
|
| pubmed:volume |
5
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:meshHeading |
pubmed-meshheading:20927343-Actins,
pubmed-meshheading:20927343-Amino Acid Sequence,
pubmed-meshheading:20927343-Carrier Proteins,
pubmed-meshheading:20927343-Crystallography, X-Ray,
pubmed-meshheading:20927343-Dimerization,
pubmed-meshheading:20927343-Homeostasis,
pubmed-meshheading:20927343-Molecular Conformation,
pubmed-meshheading:20927343-Molecular Sequence Data,
pubmed-meshheading:20927343-Protein Binding,
pubmed-meshheading:20927343-Protein Structure, Tertiary
|
| pubmed:year |
2010
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| pubmed:articleTitle |
Crystal structure of the Formin mDia1 in autoinhibited conformation.
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| pubmed:affiliation |
Department of Biochemistry, University of Texas Southwestern Medical Center at Dallas, Texas, United States of America.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|