2l9h: Difference between revisions

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[[Image:2l9h.png|left|200px]]
==Oligomeric Structure of the Chemokine CCL5/RANTES from NMR, MS, and SAXS Data==
<StructureSection load='2l9h' size='340' side='right' caption='[[2l9h]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
== Structural highlights ==
[[2l9h]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9H OCA]. <br>
<b>Related:</b> [[1u4l|1u4l]]<br>
<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
== Publication Abstract from PubMed ==
CCL5 (RANTES) is a proinflammatory chemokine known to activate leukocytes through its receptor, CCR5. Although the monomeric form of CCL5 is sufficient to cause cell migration in vitro, CCL5's propensity for aggregation is essential for migration in vivo, T cell activation and apoptosis, and HIV entry into cells. However, there is currently no structural information on CCL5 oligomers larger than the canonical CC chemokine dimer. In this study the solution structure of a CCL5 oligomer was investigated using an integrated approach, including NMR residual dipolar couplings to determine allowed relative orientations of the component monomers, SAXS to restrict overall shape, and hydroxyl radical footprinting and NMR cross-saturation experiments to identify interface residues. The resulting model of the CCL5 oligomer provides a basis for explaining the disaggregating effect of E66 and E26 mutations and suggests mechanisms by which glycosaminoglycan binding may promote oligomer formation and facilitate cell migration in vivo.


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Oligomeric Structure of the Chemokine CCL5/RANTES from NMR, MS, and SAXS Data.,Wang X, Watson C, Sharp JS, Handel TM, Prestegard JH Structure. 2011 Aug 10;19(8):1138-48. PMID:21827949<ref>PMID:21827949</ref>
The line below this paragraph, containing "STRUCTURE_2l9h", creates the "Structure Box" on the page.
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{{STRUCTURE_2l9h|  PDB=2l9h  |  SCENE=  }}


===Oligomeric Structure of the Chemokine CCL5/RANTES from NMR, MS, and SAXS Data===
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
 
== References ==
 
<references/>
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{{ABSTRACT_PUBMED_21827949}}
 
==About this Structure==
[[2l9h]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9H OCA].
 
==Reference==
<ref group="xtra">PMID:021827949</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Handel, T M.]]
[[Category: Handel, T M.]]

Revision as of 11:37, 30 April 2014

Oligomeric Structure of the Chemokine CCL5/RANTES from NMR, MS, and SAXS DataOligomeric Structure of the Chemokine CCL5/RANTES from NMR, MS, and SAXS Data

Structural highlights

2l9h is a 4 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA.

Related: 1u4l
Activity: Glucokinase, with EC number 2.7.1.2

Publication Abstract from PubMed

CCL5 (RANTES) is a proinflammatory chemokine known to activate leukocytes through its receptor, CCR5. Although the monomeric form of CCL5 is sufficient to cause cell migration in vitro, CCL5's propensity for aggregation is essential for migration in vivo, T cell activation and apoptosis, and HIV entry into cells. However, there is currently no structural information on CCL5 oligomers larger than the canonical CC chemokine dimer. In this study the solution structure of a CCL5 oligomer was investigated using an integrated approach, including NMR residual dipolar couplings to determine allowed relative orientations of the component monomers, SAXS to restrict overall shape, and hydroxyl radical footprinting and NMR cross-saturation experiments to identify interface residues. The resulting model of the CCL5 oligomer provides a basis for explaining the disaggregating effect of E66 and E26 mutations and suggests mechanisms by which glycosaminoglycan binding may promote oligomer formation and facilitate cell migration in vivo.

Oligomeric Structure of the Chemokine CCL5/RANTES from NMR, MS, and SAXS Data.,Wang X, Watson C, Sharp JS, Handel TM, Prestegard JH Structure. 2011 Aug 10;19(8):1138-48. PMID:21827949[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Wang X, Watson C, Sharp JS, Handel TM, Prestegard JH. Oligomeric Structure of the Chemokine CCL5/RANTES from NMR, MS, and SAXS Data. Structure. 2011 Aug 10;19(8):1138-48. PMID:21827949 doi:10.1016/j.str.2011.06.001
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