Pattern and Temporal Sequence of Sulfation of CCR5 N-Terminal Peptides by Tyrosylprotein Sulfotransferase-2: An Assessment of the Effects of N-Terminal Residues Export

@article{citeulike:5093365, abstract = {CC chemokine receptor 5 (CCR5) is the receptor for several inflammatory chemokines and is a coreceptor for HIV-1. Posttranslational sulfation of tyrosines in the N-terminal regions of chemokine receptors has been shown to be important in the binding affinity for chemokine ligands. In addition, sulfation of CCR5 is crucial for mediating interactions with HIV-1 envelope protein gp120. The major sulfation pathway for peptides derived from the N-terminal domains of CCR5 and CCR8 and variations of the peptides were determined by in vitro enzymatic sulfation by tyrosylprotein sulfotranferase-2 (TPST-2), subsequent separation of products by RP-HPLC, and mass spectrometry analysis. It was found that the patterns of sulfation and the rates of sulfation for CCR5 and CCR8 depend on the number of amino acids N-terminal of Tyr-3. Results herein address previous seemingly contradictory studies and delineate the temporal sulfation of N-terminal chemokine receptor peptides.}, author = {Jen, Connie H. and Moore, Kevin L. and Leary, Julie A.}, citeulike-article-id = {5093365}, citeulike-linkout-0 = {http://dx.doi.org/10.1021/bi900285c}, citeulike-linkout-1 = {http://pubs.acs.org/doi/abs/10.1021/bi900285c}, day = {16}, doi = {10.1021/bi900285c}, journal = {Biochemistry}, keywords = {ccr5, il16, terminal}, month = {June}, number = {23}, pages = {5332--5338}, posted-at = {2009-07-08 17:36:54}, priority = {2}, title = {Pattern and Temporal Sequence of Sulfation of CCR5 N-Terminal Peptides by Tyrosylprotein Sulfotransferase-2: An Assessment of the Effects of N-Terminal Residues}, url = {http://dx.doi.org/10.1021/bi900285c}, volume = {48}, year = {2009} }

TY - JOUR ID - citeulike:5093365 L3 - citeulike-article-id:5093365 N2 - CC chemokine receptor 5 (CCR5) is the receptor for several inflammatory chemokines and is a coreceptor for HIV-1. Posttranslational sulfation of tyrosines in the N-terminal regions of chemokine receptors has been shown to be important in the binding affinity for chemokine ligands. In addition, sulfation of CCR5 is crucial for mediating interactions with HIV-1 envelope protein gp120. The major sulfation pathway for peptides derived from the N-terminal domains of CCR5 and CCR8 and variations of the peptides were determined by in vitro enzymatic sulfation by tyrosylprotein sulfotranferase-2 (TPST-2), subsequent separation of products by RP-HPLC, and mass spectrometry analysis. It was found that the patterns of sulfation and the rates of sulfation for CCR5 and CCR8 depend on the number of amino acids N-terminal of Tyr-3. Results herein address previous seemingly contradictory studies and delineate the temporal sulfation of N-terminal chemokine receptor peptides. IS - 23 JF - Biochemistry EP - 5338 TI - Pattern and Temporal Sequence of Sulfation of CCR5 N-Terminal Peptides by Tyrosylprotein Sulfotransferase-2: An Assessment of the Effects of N-Terminal Residues VL - 48 SP - 5332 KW - ccr5 KW - il16 KW - terminal AU - Jen, Connie AU - Moore, Kevin AU - Leary, Julie PY - 2009/06/16/ UR - http://dx.doi.org/10.1021/bi900285c ER -