rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
2
|
pubmed:dateCreated |
1998-5-7
|
pubmed:databankReference |
|
pubmed:abstractText |
S100B, a small acidic calcium-binding protein, is a member of the S100 protein family and is a multifunctional protein capable of binding several target molecules, such as cytoskeletal proteins and protein kinases, in a calcium-dependent manner. S100B is a homodimer of S100 beta subunits (beta beta) with a total of four calcium-binding motifs called EF hands. S100B is found abundantly in nervous tissue and has been implicated in Alzheimer's disease and Down's syndrome. Structural analysis of S100B in the calcium-bound state is required to gain a better understanding of the conformational changes that occur to S100B upon calcium binding and to elucidate the mode of recognition between S100B and its target molecules.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Feb
|
pubmed:issn |
0969-2126
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
6
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
233-41
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:9519413-Amino Acid Sequence,
pubmed-meshheading:9519413-Animals,
pubmed-meshheading:9519413-Brain Chemistry,
pubmed-meshheading:9519413-Calcium,
pubmed-meshheading:9519413-Calcium-Binding Proteins,
pubmed-meshheading:9519413-Cattle,
pubmed-meshheading:9519413-Crystallography, X-Ray,
pubmed-meshheading:9519413-Cysteine,
pubmed-meshheading:9519413-Dimerization,
pubmed-meshheading:9519413-Models, Molecular,
pubmed-meshheading:9519413-Molecular Sequence Data,
pubmed-meshheading:9519413-Nerve Growth Factors,
pubmed-meshheading:9519413-Protein Conformation,
pubmed-meshheading:9519413-S100 Proteins,
pubmed-meshheading:9519413-Sequence Alignment,
pubmed-meshheading:9519413-tau Proteins
|
pubmed:year |
1998
|
pubmed:articleTitle |
A novel mode of target recognition suggested by the 2.0 A structure of holo S100B from bovine brain.
|
pubmed:affiliation |
Department of Applied Chemistry, Faculty of Engineering, Osaka University, Japan.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|