| pubmed-article:21464278 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21464278 | lifeskim:mentions | umls-concept:C0019409 | lld:lifeskim |
| pubmed-article:21464278 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:21464278 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:21464278 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:21464278 | lifeskim:mentions | umls-concept:C1707719 | lld:lifeskim |
| pubmed-article:21464278 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:21464278 | lifeskim:mentions | umls-concept:C1999230 | lld:lifeskim |
| pubmed-article:21464278 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:21464278 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:21464278 | pubmed:dateCreated | 2011-4-20 | lld:pubmed |
| pubmed-article:21464278 | pubmed:abstractText | The small heat shock protein (sHSP) ?B-crystallin (?B) plays a key role in the cellular protection system against stress. For decades, high-resolution structural studies on heterogeneous sHSPs have been confounded by the polydisperse nature of ?B oligomers. We present an atomic-level model of full-length ?B as a symmetric 24-subunit multimer based on solid-state NMR, small-angle X-ray scattering (SAXS), and EM data. The model builds on our recently reported structure of the homodimeric ?-crystallin domain (ACD) and C-terminal IXI motif in the context of the multimer. A hierarchy of interactions contributes to build multimers of varying sizes: Interactions between two ACDs define a dimer, three dimers connected by their C-terminal regions define a hexameric unit, and variable interactions involving the N-terminal region define higher-order multimers. Within a multimer, N-terminal regions exist in multiple environments, contributing to the heterogeneity observed by NMR. Analysis of SAXS data allows determination of a heterogeneity parameter for this type of system. A mechanism of multimerization into higher-order asymmetric oligomers via the addition of up to six dimeric units to a 24-mer is proposed. The proposed asymmetric multimers explain the homogeneous appearance of ?B in negative-stain EM images and the known dynamic exchange of ?B subunits. The model of ?B provides a structural basis for understanding known disease-associated missense mutations and makes predictions concerning substrate binding and the reported fibrilogenesis of ?B. | lld:pubmed |
| pubmed-article:21464278 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21464278 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21464278 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21464278 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21464278 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21464278 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21464278 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21464278 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21464278 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21464278 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:21464278 | pubmed:issn | 1091-6490 | lld:pubmed |
| pubmed-article:21464278 | pubmed:author | pubmed-author:OschkinatHart... | lld:pubmed |
| pubmed-article:21464278 | pubmed:author | pubmed-author:RajagopalPonn... | lld:pubmed |
| pubmed-article:21464278 | pubmed:author | pubmed-author:KlevitRachel... | lld:pubmed |
| pubmed-article:21464278 | pubmed:author | pubmed-author:GonenTamirT | lld:pubmed |
| pubmed-article:21464278 | pubmed:author | pubmed-author:BardiauxBenja... | lld:pubmed |
| pubmed-article:21464278 | pubmed:author | pubmed-author:JehleStefanS | lld:pubmed |
| pubmed-article:21464278 | pubmed:author | pubmed-author:VollmarBreann... | lld:pubmed |
| pubmed-article:21464278 | pubmed:author | pubmed-author:DoveKatja KKK | lld:pubmed |
| pubmed-article:21464278 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21464278 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:21464278 | pubmed:volume | 108 | lld:pubmed |
| pubmed-article:21464278 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21464278 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21464278 | pubmed:pagination | 6409-14 | lld:pubmed |
| pubmed-article:21464278 | pubmed:dateRevised | 2011-10-19 | lld:pubmed |
| pubmed-article:21464278 | pubmed:meshHeading | pubmed-meshheading:21464278... | lld:pubmed |
| pubmed-article:21464278 | pubmed:meshHeading | pubmed-meshheading:21464278... | lld:pubmed |
| pubmed-article:21464278 | pubmed:meshHeading | pubmed-meshheading:21464278... | lld:pubmed |
| pubmed-article:21464278 | pubmed:meshHeading | pubmed-meshheading:21464278... | lld:pubmed |
| pubmed-article:21464278 | pubmed:meshHeading | pubmed-meshheading:21464278... | lld:pubmed |
| pubmed-article:21464278 | pubmed:meshHeading | pubmed-meshheading:21464278... | lld:pubmed |
| pubmed-article:21464278 | pubmed:meshHeading | pubmed-meshheading:21464278... | lld:pubmed |
| pubmed-article:21464278 | pubmed:meshHeading | pubmed-meshheading:21464278... | lld:pubmed |
| pubmed-article:21464278 | pubmed:meshHeading | pubmed-meshheading:21464278... | lld:pubmed |
| pubmed-article:21464278 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21464278 | pubmed:articleTitle | N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity. | lld:pubmed |
| pubmed-article:21464278 | pubmed:affiliation | Department of Biochemistry, University of Washington, Seattle, WA 98195, USA. | lld:pubmed |
| pubmed-article:21464278 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21464278 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:21464278 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| entrez-gene:1410 | entrezgene:pubmed | pubmed-article:21464278 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:21464278 | lld:entrezgene |
