期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 359, 期 5, 页码 1400-1409出版社
ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2006.04.052
关键词
GPCR; tyrosine sulfonation; NMR; post-translational modification; HIV co-receptor
资金
- NIAID NIH HHS [AI058072, R37 AI058072, R01 AI058072-02, R01 AI058072] Funding Source: Medline
Tyrosine sulfation of the chemokine receptor CXCR4 enhances its interaction with the chemokine SDF-1 alpha. 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-1 alpha with low micromolar affinities. NMR and fluorescence polarization measurements showed that the CXCR4 peptide stabilizes dimeric SDF-1 alpha, and that sulfotyrosine 21 binds a specific site on the chemokine that includes arginine 47. We conclude that the SDF-1 alpha 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. (c) 2006 Elsevier Ltd. All rights reserved.
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