| pubmed-article:12486712 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12486712 | lifeskim:mentions | umls-concept:C1257890 | lld:lifeskim |
| pubmed-article:12486712 | lifeskim:mentions | umls-concept:C0037949 | lld:lifeskim |
| pubmed-article:12486712 | lifeskim:mentions | umls-concept:C0250604 | lld:lifeskim |
| pubmed-article:12486712 | lifeskim:mentions | umls-concept:C0282554 | lld:lifeskim |
| pubmed-article:12486712 | lifeskim:mentions | umls-concept:C0538075 | lld:lifeskim |
| pubmed-article:12486712 | lifeskim:mentions | umls-concept:C1707455 | lld:lifeskim |
| pubmed-article:12486712 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:12486712 | pubmed:dateCreated | 2002-12-17 | lld:pubmed |
| pubmed-article:12486712 | pubmed:abstractText | The eotaxin group chemokines (eotaxin, eotaxin-2, and eotaxin-3) share only 35-41% sequence identity but are all agonists for the receptor CCR3. Here we present a detailed comparison between the backbone dynamics of these three chemokines. The dynamics of eotaxin-2 were determined from 15N NMR relaxation data and compared to those obtained previously for eotaxin and eotaxin-3. For all three chemokines, the majority of residues in the first two beta-strands and the alpha-helix show highly restricted motions on the subnanosecond time scale but there is dramatically higher flexibility in the N- and C-terminal regions and also substantial mobility for residues in the N-loop region and the third beta-strand. The latter two regions form a groove on the chemokine surface that is the likely binding site for the N-terminal region of the receptor. Taken together, the available data suggest a model in which conformational rearrangements of both the chemokine and the receptor are likely to occur during binding and receptor activation. | lld:pubmed |
| pubmed-article:12486712 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12486712 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12486712 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12486712 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12486712 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12486712 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12486712 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12486712 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12486712 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12486712 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12486712 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12486712 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12486712 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12486712 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12486712 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:12486712 | pubmed:issn | 1097-0134 | lld:pubmed |
| pubmed-article:12486712 | pubmed:author | pubmed-author:StoneMartin... | lld:pubmed |
| pubmed-article:12486712 | pubmed:author | pubmed-author:MayerKristen... | lld:pubmed |
| pubmed-article:12486712 | pubmed:copyrightInfo | Copyright 2002 Wiley-Liss, Inc. | lld:pubmed |
| pubmed-article:12486712 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:12486712 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:12486712 | pubmed:volume | 50 | lld:pubmed |
| pubmed-article:12486712 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12486712 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12486712 | pubmed:pagination | 184-91 | lld:pubmed |
| pubmed-article:12486712 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:12486712 | pubmed:meshHeading | pubmed-meshheading:12486712... | lld:pubmed |
| pubmed-article:12486712 | pubmed:meshHeading | pubmed-meshheading:12486712... | lld:pubmed |
| pubmed-article:12486712 | pubmed:meshHeading | pubmed-meshheading:12486712... | lld:pubmed |
| pubmed-article:12486712 | pubmed:meshHeading | pubmed-meshheading:12486712... | lld:pubmed |
| pubmed-article:12486712 | pubmed:meshHeading | pubmed-meshheading:12486712... | lld:pubmed |
| pubmed-article:12486712 | pubmed:meshHeading | pubmed-meshheading:12486712... | lld:pubmed |
| pubmed-article:12486712 | pubmed:meshHeading | pubmed-meshheading:12486712... | lld:pubmed |
| pubmed-article:12486712 | pubmed:meshHeading | pubmed-meshheading:12486712... | lld:pubmed |
| pubmed-article:12486712 | pubmed:meshHeading | pubmed-meshheading:12486712... | lld:pubmed |
| pubmed-article:12486712 | pubmed:meshHeading | pubmed-meshheading:12486712... | lld:pubmed |
| pubmed-article:12486712 | pubmed:meshHeading | pubmed-meshheading:12486712... | lld:pubmed |
| pubmed-article:12486712 | pubmed:meshHeading | pubmed-meshheading:12486712... | lld:pubmed |
| pubmed-article:12486712 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12486712 | pubmed:articleTitle | Backbone dynamics of the CC-chemokine eotaxin-2 and comparison among the eotaxin group chemokines. | lld:pubmed |
| pubmed-article:12486712 | pubmed:affiliation | Department of Chemistry, Indiana University, Bloomington, Indiana 47405-0001, USA. | lld:pubmed |
| pubmed-article:12486712 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12486712 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:12486712 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12486712 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:12486712 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12486712 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12486712 | lld:pubmed |
