Source:http://linkedlifedata.com/resource/pubmed/id/12486712
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2002-12-17
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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.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CCL11 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CCL24 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CCL26 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CCR3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Chemokine CCL11,
http://linkedlifedata.com/resource/pubmed/chemical/Chemokine CCL24,
http://linkedlifedata.com/resource/pubmed/chemical/Chemokines, CC,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, CCR3,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Chemokine
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1097-0134
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 2002 Wiley-Liss, Inc.
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
50
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
184-91
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:12486712-Binding Sites,
pubmed-meshheading:12486712-Chemokine CCL11,
pubmed-meshheading:12486712-Chemokine CCL24,
pubmed-meshheading:12486712-Chemokines, CC,
pubmed-meshheading:12486712-Diffusion,
pubmed-meshheading:12486712-Models, Molecular,
pubmed-meshheading:12486712-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:12486712-Pliability,
pubmed-meshheading:12486712-Protein Structure, Secondary,
pubmed-meshheading:12486712-Receptors, CCR3,
pubmed-meshheading:12486712-Receptors, Chemokine,
pubmed-meshheading:12486712-Rotation
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pubmed:year |
2003
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pubmed:articleTitle |
Backbone dynamics of the CC-chemokine eotaxin-2 and comparison among the eotaxin group chemokines.
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pubmed:affiliation |
Department of Chemistry, Indiana University, Bloomington, Indiana 47405-0001, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
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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