Source:http://linkedlifedata.com/resource/pubmed/id/10806091
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2000-7-17
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pubmed:abstractText |
Several quasi-ordered arrays and three two-dimensional crystal forms of annexin VI were obtained on artificial lipid monolayers. Three-dimensional reconstructions of the crystal forms exhibit marked differences in the orientations of the two lobes, revealing flexibility of the linker between the two lobes of annexin VI. Evidence is presented that the lobes may bind the monolayer in a parallel orientation, or an antiparallel orientation, in which the second lobe is turned away from the monolayer. It is hypothesized that annexin VI may also adopt several conformations in vivo, underlying different functional roles.
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pubmed:grant | |
pubmed:keyword | |
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 |
May
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pubmed:issn |
1047-8477
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 2000 Academic Press.
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pubmed:issnType |
Print
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pubmed:volume |
130
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
54-62
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10806091-Animals,
pubmed-meshheading:10806091-Annexin A6,
pubmed-meshheading:10806091-Cattle,
pubmed-meshheading:10806091-Crystallography, X-Ray,
pubmed-meshheading:10806091-Image Processing, Computer-Assisted,
pubmed-meshheading:10806091-Microscopy, Electron,
pubmed-meshheading:10806091-Models, Molecular,
pubmed-meshheading:10806091-Protein Conformation
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pubmed:year |
2000
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pubmed:articleTitle |
Membrane-bound 3D structures reveal the intrinsic flexibility of annexin VI.
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pubmed:affiliation |
Department of Pharmacology, University of Virginia, Charlottesville, Virginia 22901, USA. AJAvila-Sakar@lbl.gov
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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