Source:http://linkedlifedata.com/resource/pubmed/id/10481916
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1999-9-23
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pubmed:abstractText |
Spectrin is a vital component of the cytoskeleton, conferring flexibility on cells and providing a scaffold for a variety of proteins. It is composed of tandem, antiparallel coiled-coil repeats. We report four related crystal structures at 1.45 A, 2.0 A, 3.1 A, and 4.0 A resolution of two connected repeats of chicken brain alpha-spectrin. In all of the structures, the linker region between adjacent units is alpha-helical without breaks, kinks, or obvious boundaries. Two features observed in the structures are (1) conformational rearrangement in one repeat, resulting in movement of the position of a loop, and (2) varying degrees of bending at the linker region. These features form the basis of two different models of flexibility: a conformational rearrangement and a bending model. These models provide novel atomic details of spectrin flexibility.
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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 |
Aug
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pubmed:issn |
0092-8674
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
98
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
523-35
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10481916-Amino Acid Sequence,
pubmed-meshheading:10481916-Amino Acid Substitution,
pubmed-meshheading:10481916-Animals,
pubmed-meshheading:10481916-Brain Chemistry,
pubmed-meshheading:10481916-Chickens,
pubmed-meshheading:10481916-Crystallography, X-Ray,
pubmed-meshheading:10481916-Models, Molecular,
pubmed-meshheading:10481916-Molecular Sequence Data,
pubmed-meshheading:10481916-Motion,
pubmed-meshheading:10481916-Nerve Tissue Proteins,
pubmed-meshheading:10481916-Protein Conformation,
pubmed-meshheading:10481916-Protein Structure, Secondary,
pubmed-meshheading:10481916-Recombinant Fusion Proteins,
pubmed-meshheading:10481916-Repetitive Sequences, Amino Acid,
pubmed-meshheading:10481916-Spectrin
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pubmed:year |
1999
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pubmed:articleTitle |
Structures of two repeats of spectrin suggest models of flexibility.
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pubmed:affiliation |
Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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