| pubmed-article:16698282 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16698282 | lifeskim:mentions | umls-concept:C0026339 | lld:lifeskim |
| pubmed-article:16698282 | lifeskim:mentions | umls-concept:C0026336 | lld:lifeskim |
| pubmed-article:16698282 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:16698282 | lifeskim:mentions | umls-concept:C0917705 | lld:lifeskim |
| pubmed-article:16698282 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:16698282 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:16698282 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:16698282 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:16698282 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:16698282 | pubmed:dateCreated | 2006-8-28 | lld:pubmed |
| pubmed-article:16698282 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698282 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698282 | pubmed:abstractText | Alpha-actinin belongs to the spectrin family of actin crosslinking and bundling proteins that function as key regulators of cell motility, morphology and adhesion. The actin-binding domain (ABD) of these proteins consists of two consecutive calponin homology (CH) domains. Electron microscopy studies on ABDs appear to support two competing actin-binding models, extended and compact, whereas the crystal structures typically display a compact conformation. We have determined the 1.7A resolution structure of the ABD of alpha-actinin 1, a ubiquitously expressed isoform. The structure displays the classical compact conformation. We evaluated the two binding models by surface conservation analysis. The results show a conserved surface that spans both domains and corresponds to two previously identified actin-binding sites (ABS2 and ABS3). A third, and probably less important site, ABS1, is mostly buried in the compact conformation. However, a thorough examination of existing structures suggests a weak and semi-polar binding interface between the two CHs, leaving open the possibility of domain reorientation or opening. Our results are consistent with a two-step binding mechanism in which the ABD interacts first in the compact form observed in the structures, and then transitions toward a higher affinity state, possibly through minor rearrangement of the domains. | lld:pubmed |
| pubmed-article:16698282 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698282 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16698282 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698282 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16698282 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698282 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698282 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16698282 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:16698282 | pubmed:issn | 1047-8477 | lld:pubmed |
| pubmed-article:16698282 | pubmed:author | pubmed-author:YuLiL | lld:pubmed |
| pubmed-article:16698282 | pubmed:author | pubmed-author:DominguezRobe... | lld:pubmed |
| pubmed-article:16698282 | pubmed:author | pubmed-author:FerronFrançoi... | lld:pubmed |
| pubmed-article:16698282 | pubmed:author | pubmed-author:LeeSung... | lld:pubmed |
| pubmed-article:16698282 | pubmed:author | pubmed-author:KerffFrederic... | lld:pubmed |
| pubmed-article:16698282 | pubmed:author | pubmed-author:Borrego-DiazE... | lld:pubmed |
| pubmed-article:16698282 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16698282 | pubmed:volume | 155 | lld:pubmed |
| pubmed-article:16698282 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16698282 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16698282 | pubmed:pagination | 230-8 | lld:pubmed |
| pubmed-article:16698282 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:16698282 | pubmed:meshHeading | pubmed-meshheading:16698282... | lld:pubmed |
| pubmed-article:16698282 | pubmed:meshHeading | pubmed-meshheading:16698282... | lld:pubmed |
| pubmed-article:16698282 | pubmed:meshHeading | pubmed-meshheading:16698282... | lld:pubmed |
| pubmed-article:16698282 | pubmed:meshHeading | pubmed-meshheading:16698282... | lld:pubmed |
| pubmed-article:16698282 | pubmed:meshHeading | pubmed-meshheading:16698282... | lld:pubmed |
| pubmed-article:16698282 | pubmed:meshHeading | pubmed-meshheading:16698282... | lld:pubmed |
| pubmed-article:16698282 | pubmed:meshHeading | pubmed-meshheading:16698282... | lld:pubmed |
| pubmed-article:16698282 | pubmed:meshHeading | pubmed-meshheading:16698282... | lld:pubmed |
| pubmed-article:16698282 | pubmed:meshHeading | pubmed-meshheading:16698282... | lld:pubmed |
| pubmed-article:16698282 | pubmed:meshHeading | pubmed-meshheading:16698282... | lld:pubmed |
| pubmed-article:16698282 | pubmed:meshHeading | pubmed-meshheading:16698282... | lld:pubmed |
| pubmed-article:16698282 | pubmed:meshHeading | pubmed-meshheading:16698282... | lld:pubmed |
| pubmed-article:16698282 | pubmed:meshHeading | pubmed-meshheading:16698282... | lld:pubmed |
| pubmed-article:16698282 | pubmed:meshHeading | pubmed-meshheading:16698282... | lld:pubmed |
| pubmed-article:16698282 | pubmed:meshHeading | pubmed-meshheading:16698282... | lld:pubmed |
| pubmed-article:16698282 | pubmed:meshHeading | pubmed-meshheading:16698282... | lld:pubmed |
| pubmed-article:16698282 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16698282 | pubmed:articleTitle | Crystal structure of the actin-binding domain of alpha-actinin 1: evaluating two competing actin-binding models. | lld:pubmed |
| pubmed-article:16698282 | pubmed:affiliation | Boston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472, USA. | lld:pubmed |
| pubmed-article:16698282 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16698282 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:16698282 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16698282 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16698282 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16698282 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16698282 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16698282 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16698282 | lld:pubmed |
