Recognition of a CXCR4 Sulfotyrosine by the Chemokine Stromal Cell-derived Factor-1[alpha] (SDF-1[alpha]/CXCL12) Export

@article{citeulike:3125477, abstract = {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.}, author = {Veldkamp, Christopher T. and Seibert, Christoph and Peterson, Francis C. and Sakmar, Thomas P. and Volkman, Brian F.}, citeulike-article-id = {3125477}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.jmb.2006.04.052}, citeulike-linkout-1 = {http://www.sciencedirect.com/science/article/B6WK7-4JXRHXK-2/2/66c7d7f4106310d196fcb63e546d3c93}, day = {23}, doi = {10.1016/j.jmb.2006.04.052}, journal = {Journal of Molecular Biology}, keywords = {cxcr4, tys}, month = {June}, number = {5}, pages = {1400--1409}, posted-at = {2008-08-15 11:42:01}, priority = {2}, title = {Recognition of a CXCR4 Sulfotyrosine by the Chemokine Stromal Cell-derived Factor-1[alpha] (SDF-1[alpha]/CXCL12)}, url = {http://dx.doi.org/10.1016/j.jmb.2006.04.052}, volume = {359}, year = {2006} }

TY - JOUR ID - citeulike:3125477 L3 - citeulike-article-id:3125477 N2 - 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. IS - 5 JF - Journal of Molecular Biology EP - 1409 TI - Recognition of a CXCR4 Sulfotyrosine by the Chemokine Stromal Cell-derived Factor-1[alpha] (SDF-1[alpha]/CXCL12) VL - 359 SP - 1400 KW - cxcr4 KW - tys AU - Veldkamp, Christopher AU - Seibert, Christoph AU - Peterson, Francis AU - Sakmar, Thomas AU - Volkman, Brian PY - 2006/06/23/ UR - http://dx.doi.org/10.1016/j.jmb.2006.04.052 ER -