|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
11
|
|
pubmed:dateCreated |
2006-10-31
|
|
pubmed:abstractText |
SDF-1alpha is a member of the chemokine family implicated in various reactions in the immune system. The interaction of SDF-1alpha with its receptor, CXCR4, is responsible for metastasis of a variety of cancers. SDF-1alpha is also known to play a role in HIV-1 pathogenesis. The structures of SDF-1alpha determined by NMR spectroscopy have been shown to be monomeric while X-ray structures are dimeric. Biochemical data and in vivo studies suggest that dimerization is likely to be important for the function of chemokines. We report here the dynamics of SDF-1alpha determined through measurement of main chain (15)N NMR relaxation data. The data were obtained at several concentrations of SDF-1alpha and used to determine a dimerization constant of approximately 5 mM for a monomer-dimer equilibrium. The dimerization constant was subsequently used to extrapolate values for the relaxation data corresponding to monomeric SDF-1alpha. The experimental relaxation data and the extrapolated data for monomeric SDF-1alpha were analyzed using the model free approach. The model free analysis indicated that SDF-1alpha is rigid on the nano- to picosecond timescale with flexible termini. Several residues involved in the dimer interface display slow micro- to millisecond timescale motions attributable to chemical exchange such as monomer-dimer equilibrium. NMR relaxation measurements are shown to be applicable for studying oligomerization processes such as the dimerization of SDF-1alpha.
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-10504268,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-10526406,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-10548050,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-10656804,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-10954912,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-10966641,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-11242036,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-11281710,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-11425309,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-11456835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-11513585,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-11556308,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-11601978,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-1168493,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-11785755,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-11807180,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-11859767,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-12486712,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-12489421,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-12548571,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-12571364,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-12626353,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-12848986,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-14595012,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-15516962,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-15588815,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-15607894,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-15741341,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-16140327,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-16650056,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-7539012,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-7812156,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-7850167,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-8140420,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-8464050,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-8709256,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-9054979,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-9194185,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-9384579,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-9560152,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-9600847,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-9618518,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-9634237,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-9634238,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-9671557,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17075134-9931005
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Nov
|
|
pubmed:issn |
0961-8368
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
15
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
2568-78
|
|
pubmed:dateRevised |
2009-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:17075134-Amino Acid Sequence,
pubmed-meshheading:17075134-Chemokine CXCL12,
pubmed-meshheading:17075134-Chemokines,
pubmed-meshheading:17075134-Chemokines, CXC,
pubmed-meshheading:17075134-Dimerization,
pubmed-meshheading:17075134-Humans,
pubmed-meshheading:17075134-Models, Molecular,
pubmed-meshheading:17075134-Models, Theoretical,
pubmed-meshheading:17075134-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:17075134-Osmolar Concentration,
pubmed-meshheading:17075134-Protein Binding
|
|
pubmed:year |
2006
|
|
pubmed:articleTitle |
Backbone dynamics of SDF-1alpha determined by NMR: interpretation in the presence of monomer-dimer equilibrium.
|
|
pubmed:affiliation |
Department of Biochemistry and Protein Engineering Network of Centres of Excellence, University of Alberta, Edmonton, Alberta T6G 2S2, Canada.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
