| pubmed-article:16725153 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16725153 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:16725153 | lifeskim:mentions | umls-concept:C0282554 | lld:lifeskim |
| pubmed-article:16725153 | lifeskim:mentions | umls-concept:C1332817 | lld:lifeskim |
| pubmed-article:16725153 | lifeskim:mentions | umls-concept:C1332823 | lld:lifeskim |
| pubmed-article:16725153 | lifeskim:mentions | umls-concept:C0077556 | lld:lifeskim |
| pubmed-article:16725153 | lifeskim:mentions | umls-concept:C1955901 | lld:lifeskim |
| pubmed-article:16725153 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:16725153 | pubmed:dateCreated | 2006-6-21 | lld:pubmed |
| pubmed-article:16725153 | pubmed:abstractText | Tyrosine sulfation of the chemokine receptor CXCR4 enhances its interaction with the chemokine SDF-1alpha. Given similar post-translational modification of other receptors, including CCR5, CX3CR1 and CCR2b, tyrosine sulfation may be of universal importance in chemokine signaling. N-terminal domains from seven transmembrane chemokine receptors have been employed for structural studies of chemokine-receptor interactions, but never in the context of proper post-translational modifications known to affect function. A CXCR4 peptide modified at position 21 by expressed tyrosylprotein sulfotransferase-1 and unmodified peptide are both disordered in solution, but bind SDF-1alpha with low micromolar affinities. NMR and fluorescence polarization measurements showed that the CXCR4 peptide stabilizes dimeric SDF-1alpha, and that sulfotyrosine 21 binds a specific site on the chemokine that includes arginine 47. We conclude that the SDF-1alpha dimer preferentially interacts with receptor peptide, and residues beyond the extreme N-terminal region of CXCR4, including sulfotyrosine 21, make specific contacts with the chemokine ligand. | lld:pubmed |
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| pubmed-article:16725153 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16725153 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16725153 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16725153 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16725153 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:16725153 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:16725153 | pubmed:author | pubmed-author:SakmarThomas... | lld:pubmed |
| pubmed-article:16725153 | pubmed:author | pubmed-author:VolkmanBrian... | lld:pubmed |
| pubmed-article:16725153 | pubmed:author | pubmed-author:SeibertChrist... | lld:pubmed |
| pubmed-article:16725153 | pubmed:author | pubmed-author:PetersonFranc... | lld:pubmed |
| pubmed-article:16725153 | pubmed:author | pubmed-author:VeldkampChris... | lld:pubmed |
| pubmed-article:16725153 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16725153 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:16725153 | pubmed:volume | 359 | lld:pubmed |
| pubmed-article:16725153 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16725153 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16725153 | pubmed:pagination | 1400-9 | lld:pubmed |
| pubmed-article:16725153 | pubmed:dateRevised | 2011-5-5 | lld:pubmed |
| pubmed-article:16725153 | pubmed:meshHeading | pubmed-meshheading:16725153... | lld:pubmed |
| pubmed-article:16725153 | pubmed:meshHeading | pubmed-meshheading:16725153... | lld:pubmed |
| pubmed-article:16725153 | pubmed:meshHeading | pubmed-meshheading:16725153... | lld:pubmed |
| pubmed-article:16725153 | pubmed:meshHeading | pubmed-meshheading:16725153... | lld:pubmed |
| pubmed-article:16725153 | pubmed:meshHeading | pubmed-meshheading:16725153... | lld:pubmed |
| pubmed-article:16725153 | pubmed:meshHeading | pubmed-meshheading:16725153... | lld:pubmed |
| pubmed-article:16725153 | pubmed:meshHeading | pubmed-meshheading:16725153... | lld:pubmed |
| pubmed-article:16725153 | pubmed:meshHeading | pubmed-meshheading:16725153... | lld:pubmed |
| pubmed-article:16725153 | pubmed:meshHeading | pubmed-meshheading:16725153... | lld:pubmed |
| pubmed-article:16725153 | pubmed:meshHeading | pubmed-meshheading:16725153... | lld:pubmed |
| pubmed-article:16725153 | pubmed:meshHeading | pubmed-meshheading:16725153... | lld:pubmed |
| pubmed-article:16725153 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16725153 | pubmed:articleTitle | Recognition of a CXCR4 sulfotyrosine by the chemokine stromal cell-derived factor-1alpha (SDF-1alpha/CXCL12). | lld:pubmed |
| pubmed-article:16725153 | pubmed:affiliation | Department of Biochemistry, Medical College of Wisconsin, Milwaukee, 53226, USA. | lld:pubmed |
| pubmed-article:16725153 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16725153 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16725153 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
